Information on EC 3.1.3.1 - alkaline phosphatase

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The expected taxonomic range for this enzyme is: Archaea, Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.1.3.1
-
RECOMMENDED NAME
GeneOntology No.
alkaline phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
Q9UZV2
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, active site structure, highly conserved in evolution of alkaline phosphatases
P05187
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, active site structure, mechanism
shrimp
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, catalytically active His153 and His328
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate, substrate binding and active site structure
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Arg166 contributes to catalysis through binding interactions and through additional transition state stabilization that may arise from complementarity of the guanidinum group to the geometry of the trigonal bipyramidal transition state
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
double in-line displacement mechanism involving two-metal ion catalysis
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
Wide specificity. Also catalyses transphosphorylations. Some enzymes hydrolyse diphosphate
Neurospora crassa St. L. 74A, Saccharomyces cerevisiae 257, Serratia marcescens 211, Thermus sp. 314, Ulva pertusa Kjelm, Vibrio sp. 2P44
-
-
a phosphate monoester + H2O = an alcohol + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
phosphomonoester
-
PATHWAY
KEGG Link
MetaCyc Link
Aminobenzoate degradation
-
diethylphosphate degradation
-
Folate biosynthesis
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
SYSTEMATIC NAME
IUBMB Comments
phosphate-monoester phosphohydrolase (alkaline optimum)
Wide specificity. Also catalyses transphosphorylations. The human placental enzyme is a zinc protein. Some enzymes hydrolyse diphosphate (cf. EC 3.6.1.1 inorganic diphosphatase)
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
alkaline phenyl phosphatase
-
-
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
Q9KWY4
-
alkaline phosphatase
-
-
alkaline phosphatase
P19111
-
alkaline phosphatase
A3ZF85
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
P00634
-
alkaline phosphatase
-
-
alkaline phosphatase
Q92058
-
alkaline phosphatase
C1K6P2
-
alkaline phosphatase
A8WEG4
-
alkaline phosphatase
-
-
alkaline phosphatase
B0R9W3
-
alkaline phosphatase
Halomonas sp.
-
-
alkaline phosphatase
B4Z1D6, B4Z1D7
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
Neurospora crassa St. L. 74A
-
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
Q17TZ1
-
alkaline phosphatase
-
-
alkaline phosphatase
Q9UZV2
-
alkaline phosphatase
P08289
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
Saccharomyces cerevisiae 257
-
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
Serratia marcescens 211
-
-
-
alkaline phosphatase
shrimp
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
A1YYW7
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
Terfezia claveryi Chatin
-
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
-
-
alkaline phosphatase
Thermus sp. 314
-
-
-
alkaline phosphatase
-
-
alkaline phosphatase
Ulva pertusa Kjelm
-
-
-
alkaline phosphatase
-
-
alkaline phosphatase
Vibrio sp. 2P44
-
-
-
alkaline phosphatase
-
-
alkaline phosphatase F I
-
-
alkaline phosphatase F II
-
-
alkaline phosphatase HaALP1
B4Z1D6
-
alkaline phosphatase HaALP2
B4Z1D7
-
alkaline phosphatase HvmALP 1
C3U1V9
-
alkaline phosphatase HvmALP 2
C3U1W0
-
alkaline phosphatase HvmALP 3
C3U1W1
-
alkaline phosphatase HvmALP 4
C3U1W2
-
alkaline phosphatase HvmALP 5
B4X983
-
alkaline phosphatase VI-1
-
-
alkaline phosphohydrolase
-
-
-
-
alkaline phosphomonoesterase
-
-
-
-
all2843
-
-
ALP
-
-
-
-
ALP
P19111
-
ALP
Q17TZ1
-
ALP
-
bone isoform; intestinal isoform; liver isoform
ALP
P08289
liver isoform
ALP
Ulva pertusa Kjelm
-
-
-
ALPase
-
-
ALPase
Saccharomyces cerevisiae 257
-
-
-
ALPP
-
-
alr5291
-
alr5291 encodes a protein that is an atypical alkaline phosphatase like other cyanobacteria PhoAs
AP
shrimp
-
-
AP
Thermus sp. 314
-
-
-
AP-TNAP
-
-
-
-
APase
-
-
-
-
APase
-
-
APase
Serratia marcescens 211
-
-
-
APASED
-
-
-
-
atypical purple alkaline phosphatase
B4EKR2
-
BALP
-
-
BC6
-
-
-
-
BIALP
-
-
BIAP
-
-
bone alkaline phosphatase
-
-
bone specific alkaline phosphatase
-
-
calf intestinal alkaline phosphatase
-
-
CAP
-
-
CAPase
Serratia marcescens 211
-
-
-
CIAP
-
-
EAP
-
-
-
-
extracellular alkaline phosphatase
Chenopodium rubrum
-
-
germ cell alkaline phosphatase
-
-
Germ-cell alkaline phosphatase
-
-
-
-
glycerophosphatase
-
-
-
-
H-AP
-
-
-
-
H-AP
-
high-molecular weight alkaline phosphatase
H-AP
Pseudomonas aeruginosa H103
-
high-molecular weight alkaline phosphatase
-
HaALP
Halomonas sp.
-
-
HaALP
Halomonas sp. 593
-
-
-
HaALP
B4Z1D6, B4Z1D7
-
high molecular weight alkaline phosphatase
-
-
High molecular weight phosphatase
-
-
-
-
IAP
-
-
-
-
IAPase
Serratia marcescens 211
-
-
-
intestinal alkaline phosphatase
P19111
-
intestinal alkaline phosphatase
-
-
intestinal alkaline phosphatase
-
-
L-AP
-
-
-
-
L-AP
-
low-molecular weight alkaline phosphatase
L-AP
Pseudomonas aeruginosa H103
-
low-molecular weight alkaline phosphatase
-
Liver/bone/kidney isozyme
-
-
-
-
low molecular weight alkaline phosphatase
-
-
Low molecular weight phosphatase
-
-
-
-
M-ALP
-
-
-
-
Nagao isozyme
-
-
-
-
Nl-ALP1
-
soluble protein
Nl-ALP2
-
insoluble memrane-bound protein
non-specific alkaline phosphatase
-
-
-
-
OE5192R
B0R9W3
gene coding for HSAP
orthophosphoric-mono phosphohydrolase
-
-
PALP
-
-
PHO13
-
gene name
PHO8
-
gene name
phosphatase, alkaline
-
-
-
-
phosphomonoesterase
-
-
-
-
phox
Pasteurella multocida X-73
A1C3J6
-
-
placental alkaline phosphatase
-
-
PLAP-like
-
-
-
-
purple acid phosphatase-like protein
B4EKR2
-
RAN1
-
-
-
-
Regan isozyme
-
-
-
-
rTL2
P08289
-
SAP
shrimp
-
-
SEAP
-
-
secreted alkaline phosphatase
-
-
semen plasma alkaline phosphatase
-
-
seminal plasma alkaline phosphatase
-
-
seminal plasma AP
-
-
SmAP
A8TKU6
-
TAB5 AP
Q9KWY4
-
tissue non-specific alkaline phosphatase
-
-
tissue nonspecific alkaline phosphatase
-
-
tissue-nonspecific alkaline phosphatase
P09487
-
tissue-nonspecific alkaline phosphatase
-
-
tissue-nonspecific alkaline phosphatase
-
-
tissue-nonspecific alkaline phosphatase
P05186
-
tissue-nonspecific alkaline phosphatase
-
-
tissue-nonspecific ALP
-
-
tissue-specific intestinal ALP type II
-
-
TNAP
-
-
TNAP
P09487
-
TNAP
P05186
-
TNAP
-
-
TNSALP
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-78-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain K1
-
-
Manually annotated by BRENDA team
antarctic bacterium
strain HK47
-
-
Manually annotated by BRENDA team
antarctic bacterium
strain TAB5
-
-
Manually annotated by BRENDA team
antarctic bacterium HK47
strain HK47
-
-
Manually annotated by BRENDA team
three isoenzymes: I, II, III
-
-
Manually annotated by BRENDA team
alkaline phosphatase F I; alkaline phosphatase F II
-
-
Manually annotated by BRENDA team
Bacillus licheniformis MC14
strain MC14
-
-
Manually annotated by BRENDA team
strain P9
-
-
Manually annotated by BRENDA team
Bacillus sp. OK-1
-
-
-
Manually annotated by BRENDA team
strain P9
-
-
Manually annotated by BRENDA team
2 isoenzymes from calf: C1 and C2, one isoenzyme from adult B2; calf
-
-
Manually annotated by BRENDA team
strain J2315
UniProt
Manually annotated by BRENDA team
CBS 6947
-
-
Manually annotated by BRENDA team
Candida tropicalis CBS 6947
CBS 6947
-
-
Manually annotated by BRENDA team
beagle and mixed breed, 2 genes encoding 2 isozyme types: a tissue non-specific isozyme and an intestinal isozyme
-
-
Manually annotated by BRENDA team
Chenopodium rubrum
-
-
-
Manually annotated by BRENDA team
strain KMM MC-296
-
-
Manually annotated by BRENDA team
Cobetia marina KMM MC-296
strain KMM MC-296
-
-
Manually annotated by BRENDA team
Syrian hamster
-
-
Manually annotated by BRENDA team
gene alp
-
-
Manually annotated by BRENDA team
stallion
-
-
Manually annotated by BRENDA team
gene phoA
-
-
Manually annotated by BRENDA team
gene phoA
UniProt
Manually annotated by BRENDA team
gene phoA, 3 isozymes 1,2, and 3 differing in the N-terminal sequence; gene phoA, 3 isozymes 1, 2, and 3 differing in the N-terminal sequence
-
-
Manually annotated by BRENDA team
K12 strain 706, a periplasmic-excretory mutant
-
-
Manually annotated by BRENDA team
several isoenzymes
-
-
Manually annotated by BRENDA team
strain C4F1
-
-
Manually annotated by BRENDA team
Escherichia coli C4F1
strain C4F1
-
-
Manually annotated by BRENDA team
Halomonas sp.
-
-
-
Manually annotated by BRENDA team
Halomonas sp.
strain 593
-
-
Manually annotated by BRENDA team
Halomonas sp. 593
strain 593
-
-
Manually annotated by BRENDA team
4 isozyme types: 1. nonspecific liver/bone/kidney, which is also present in osteoblast and neutrophilic granulocytes, 2. intestinal, 3. placental, 4. germ-cell
-
-
Manually annotated by BRENDA team
at least 3 isoenzymes: placental, intestinal and tissue non-specific
-
-
Manually annotated by BRENDA team
humanplacenta alkaline phosphatase PLAP
Uniprot
Manually annotated by BRENDA team
precursor
UniProt
Manually annotated by BRENDA team
secreted alkaline phosphatase SEAP containing a single N-glycan chain, a model protein for investigation of glycosylation pattern
-
-
Manually annotated by BRENDA team
several isozymes
-
-
Manually annotated by BRENDA team
strain KP1
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae KP1
strain KP1
-
-
Manually annotated by BRENDA team
Micrococcus sodonensis
-
-
-
Manually annotated by BRENDA team
C57BL/6-N mice
-
-
Manually annotated by BRENDA team
four-days-old ICR mice
-
-
Manually annotated by BRENDA team
Mus musculus C57BL/6-N
C57BL/6-N mice
-
-
Manually annotated by BRENDA team
levamisole-insensitive alkaline phosphatase activity; levamisole-sensitive alkaline phosphatase activity
-
-
Manually annotated by BRENDA team
strain St. L. 74A, constitutive enzyme expression
-
-
Manually annotated by BRENDA team
wild-type strain osmotically-sensitive mutant os-1
Q7S2X3
SwissProt
Manually annotated by BRENDA team
Neurospora crassa St. L. 74A
strain St. L. 74A, constitutive enzyme expression
-
-
Manually annotated by BRENDA team
no activity in Marinovum algicola
-
-
-
Manually annotated by BRENDA team
no activity in Marinovum algicola ATCC 51442
-
-
-
Manually annotated by BRENDA team
Ophicephalus punctatus Bloch
-
-
-
Manually annotated by BRENDA team
a major intestinal-like isoenzyme and a minor tissue-unspecific type
-
-
Manually annotated by BRENDA team
strain X-73
UniProt
Manually annotated by BRENDA team
Pasteurella multocida X-73
strain X-73
UniProt
Manually annotated by BRENDA team
Porphyromonas gingivalis 381
strain 381
-
-
Manually annotated by BRENDA team
ATCC 25611
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa H103
H103
-
-
Manually annotated by BRENDA team
euryarchaeon, strain Orsay, highly thermostable enzyme
SwissProt
Manually annotated by BRENDA team
several intestinal isozymes
-
-
Manually annotated by BRENDA team
streptozotocin-induced diabetic rat
-
-
Manually annotated by BRENDA team
three subforms: 1, 2 and 3
-
-
Manually annotated by BRENDA team
substrate specific enzyme form, non specific enzyme form from structural gene PHO8, and particulate enzyme form from structural gene PHO8
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae 257
strain 257
-
-
Manually annotated by BRENDA team
Saccharomyces pombe
substrate specific enzyme form from structural gene PHO2, non specific enzyme form from structural gene PHO3 and particulate enzyme form from structural gene PHO3
-
-
Manually annotated by BRENDA team
clam, Da Costa 1778
-
-
Manually annotated by BRENDA team
thermostable conidial and mycelial alkaline phosphatases, thermophilic fungus
-
-
Manually annotated by BRENDA team
strain 211, 2 distinct enzyme forms, an inducible enzyme form IAPase in 4 isozymes, and a constitutive enzyme form CAPase
-
-
Manually annotated by BRENDA team
Serratia marcescens 211
strain 211, 2 distinct enzyme forms, an inducible enzyme form IAPase in 4 isozymes, and a constitutive enzyme form CAPase
-
-
Manually annotated by BRENDA team
shrimp
cold-adapted enzyme
-
-
Manually annotated by BRENDA team
domestica
-
-
Manually annotated by BRENDA team
Synechococcus elongatus PCC 7942 R2
strain R2
-
-
Manually annotated by BRENDA team
Terfezia claveryi Chatin
Chatin
-
-
Manually annotated by BRENDA team
strain DSM 5068
-
-
Manually annotated by BRENDA team
strain 314
-
-
Manually annotated by BRENDA team
strain T351
SwissProt
Manually annotated by BRENDA team
Thermus sp. 314
strain 314
-
-
Manually annotated by BRENDA team
strain T351
SwissProt
Manually annotated by BRENDA team
strain XM
SwissProt
Manually annotated by BRENDA team
Thermus thermophilus XM
strain XM
SwissProt
Manually annotated by BRENDA team
Kjelm
-
-
Manually annotated by BRENDA team
Ulva pertusa Kjelm
Kjelm
-
-
Manually annotated by BRENDA team
Vibrio 2P44
-
-
Manually annotated by BRENDA team
Vibrio sp. 2P44
Vibrio 2P44
-
-
Manually annotated by BRENDA team
venomous snake
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
B0R9W3, -
deletion of OE5192R produces a mutant strain with virtually no phosphatase activity
malfunction
A8TKU6
the ability of living parasites to cleave exogenous adenosine monophosphate and generate adenosine is very largely abolished when SmAP gene expression is suppressed following RNAi treatment targeting the gene
physiological function
-
Daphnia magna eating phosphorus-poor food have significantly higher alkaline phosphatase activity in their bodies compared with individuals eating phosphorus-rich food. By contrast, poor phosphorus-nutrition of Daphnia lowers alkaline phosphatase activity in released materials compared with that measured from their phosphorus-sufficient conspecifics
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2',3'-CMP + H2O
?
show the reaction diagram
-
-
-
-
?
2',3'-GMP + H2O
?
show the reaction diagram
-
-
-
-
?
2',3'-GMP + H2O
?
show the reaction diagram
-
-
-
-
?
2',3'-UMP + H2O
?
show the reaction diagram
-
-
-
-
?
2',3-AMP + H2O
?
show the reaction diagram
-
-
-
-
?
2',3-AMP + H2O
?
show the reaction diagram
-
20% of activity with p-nitrophenyl phosphate
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
2'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
-
-
-
?
2'-deoxyadenosine 5'-monophosphate + H2O
?
show the reaction diagram
O86025
113.3% of the activity with 4-nitrophenyl phosphate
-
-
?
2'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
2'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
2'-[2-benzthiazole]-6'-hydroxybenzthiazole phosphate + H2O
2'-[2-benzthiazole]-6'-hydroxybenzthiazole + phosphate
show the reaction diagram
-
weakly fluorescent substrate
highly fluorescent product
?
2,4-dinitrophenyl phosphate + H2O
2,4-dinitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate + H2O
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenol + phosphate
show the reaction diagram
-
CDP-star
-
-
?
2-glycerol phosphate + H2O
glycerol + phosphate
show the reaction diagram
Q17TZ1
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
show the reaction diagram
-
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
show the reaction diagram
-
-
-
-
?
2-naphthyl phosphate + H2O
2-naphthol + phosphate
show the reaction diagram
-
-
-
-
?
2-naphtyl phosphate + H2O
2-napthol + phosphate
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
-
2-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
hydrolyzed by isoenzyme III, weak activity with isoenzyme I and II
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
53.7% of the activity with 4-nitrophenyl phosphate
-
-
?
2-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
Q7S2X3
wild-type activity is 16.9% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 16.3fold higher than activity from wild-type enzyme
-
-
?
3'-ADP + H2O
?
show the reaction diagram
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
Saccharomyces cerevisiae 257
-
-
-
?
3'-AMP + H2O
adenosine + phosphate
show the reaction diagram
Bacillus licheniformis MC14
-
-
-
-
?
3'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
-
-
-
?
3'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
3'-ITP + H2O
?
show the reaction diagram
-
51.5% of the activity with 4-nitrophenyl phosphate
-
-
?
3'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
3-nitrobenzyl phosphate + H2O
3-nitrobenzoate + phosphate
show the reaction diagram
-
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
-
3-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
3-phosphoglycerate + H2O
glycerol + phosphate
show the reaction diagram
-
hydrolyzed by isoenzyme III, weak activity with isoenzyme II, no activity with isoenzyme I
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl phosphate + H2O
4-methylumbelliferone + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-, P00634
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
P08289
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Chenopodium rubrum
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Halomonas sp.
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-, Q9UZV2
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
O86025
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
B4Z1D6, B4Z1D7
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
A8WEG4, -
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Q17TZ1
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
P19111
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
A3ZF85, -
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Q92058
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
A1YYW7
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
P00634
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
A8TKU6
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
C1K6P2
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
B0R9W3, -
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
best substrate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
P05187
allosteric mechanism
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
non-specific, phosphoseryl intermediate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
non-specific, via phosphoseryl intermediate
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
reaction is at least partially diffusion-controlled
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Q7S2X3
activity with mutant os-1 enzyme is 12.2fold higher than activity from wild-type enzyme
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
strong support for a model in which electrostatic interactions between the bimetallo Zn2+ site and a nonbridging phosphate ester oxygen atom make a significant contribution to the large rate enhancement observed for alkaline phosphatase-catalyzed phosphate monoester hydrolysis
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Neurospora crassa St. L. 74A
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Vibrio sp. 2P44
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Terfezia claveryi Chatin
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Ulva pertusa Kjelm
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
O86025
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
Serratia marcescens 211
-
-
-
?
4-nitrophenyl sulfate + H2O
4-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
5'-ADP + H2O
?
show the reaction diagram
-
-
-
-
?
5'-ADP + H2O
?
show the reaction diagram
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
-
90% of activity with p-nitrophenyl phosphate
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
Saccharomyces cerevisiae 257
-
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
Cobetia marina KMM MC-296
-
90% of activity with p-nitrophenyl phosphate
-
-
?
5'-AMP + H2O
adenosine + phosphate
show the reaction diagram
Bacillus licheniformis MC14
-
-
-
-
?
5'-ATP + H2O
?
show the reaction diagram
-
-
-
-
?
5'-ATP + H2O
?
show the reaction diagram
-
-
-
-
?
5'-ATP + H2O
?
show the reaction diagram
-
weak
-
-
?
5'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
-
-
-
?
5'-CMP + H2O
cytidine + phosphate
show the reaction diagram
-
80% of activity with p-nitrophenyl phosphate
-
-
?
5'-CMP + H2O
cytidine + phosphate
show the reaction diagram
Bacillus licheniformis MC14
-
-
-
-
?
5'-dAMP + H2O
?
show the reaction diagram
-
-
-
-
?
5'-dCMP + H2O
deoxycytidine + phosphate
show the reaction diagram
-
80% of activity with p-nitrophenyl phosphate
-
-
?
5'-dCMP + H2O
?
show the reaction diagram
-
-
-
-
?
5'-dCMP + H2O
?
show the reaction diagram
-
-
-
-
?
5'-dGMP + H2O
?
show the reaction diagram
-
-
-
-
?
5'-dTMP + H2O
?
show the reaction diagram
-
-
-
-
?
5'-dTMP + H2O
?
show the reaction diagram
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-GMP + H2O
guanosine + phosphate
show the reaction diagram
-
40% of activity with p-nitrophenyl phosphate
-
-
?
5'-IMP + H2O
inosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-IMP + H2O
inosine + phosphate
show the reaction diagram
-
-
-
-
?
5'-TMP + H2O
thymidine + phosphate
show the reaction diagram
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
Cobetia marina, Cobetia marina KMM MC-296
-
30% of activity with p-nitrophenyl phosphate
-
-
?
5'-UMP + H2O
uridine + phosphate
show the reaction diagram
Bacillus licheniformis MC14
-
-
-
-
?
5-bromo-4-chloro-3-indolyl phosphate + H2O
?
show the reaction diagram
O86025
50.3% of the activity with 4-nitrophenyl phosphate
-
-
?
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
?
show the reaction diagram
-
-
-
-
-
acyl-CoA:cholesterol acyltransferase + H2O
?
show the reaction diagram
-
-
-
-
?
adenosine 5'-(beta-glucosyl)diphosphate + H2O
?
show the reaction diagram
-
29.8% of the activity with 4-nitrophenyl phosphate
-
-
?
adenosine 5'-diphosphate + H2O
AMP + phosphate
show the reaction diagram
-
77% of the activity with 4-nitrophenyl phosphate
-
-
?
adenosine 5'-monophosphate + H2O
?
show the reaction diagram
O86025
306.1% of the activity with 4-nitrophenyl phosphate
-
-
?
adenosine 5'-triphosphate + H2O
?
show the reaction diagram
O86025
257.4% of the activity with 4-nitrophenyl phosphate
-
-
?
adenosine 5'-triphosphate + H2O
AMP + phosphate
show the reaction diagram
-
61% of the activity with 4-nitrophenyl phosphate
-
-
?
ADP + H2O
?
show the reaction diagram
-
-
-
-
?
ADP + H2O
?
show the reaction diagram
-
-
-
-
?
ADP + H2O
?
show the reaction diagram
-
-
-
-
?
ADP + H2O
?
show the reaction diagram
-
-
-
-
?
ADP + H2O
?
show the reaction diagram
antarctic bacterium
-
-
-
-
?
ADP + H2O
?
show the reaction diagram
-
-
-
-
?
ADP + H2O
?
show the reaction diagram
-
20% of activity with p-nitrophenyl phosphate
-
-
?
ADP + H2O
?
show the reaction diagram
-
alkaline phosphatase F I, alkaline phosphatase F II
-
-
?
ADP + H2O
?
show the reaction diagram
Cobetia marina KMM MC-296
-
20% of activity with p-nitrophenyl phosphate
-
-
?
ADP + H2O
?
show the reaction diagram
antarctic bacterium HK47
-
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
-
-
-
?
ADP + H2O
AMP + phosphate
show the reaction diagram
Q7S2X3
wild-type activity is 16.9% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 1.2fold lower than activity from wild-type enzyme
-
-
?
alpha-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
60% of activity with p-nitrophenyl phosphate
-
-
?
alpha-naphthyl acid phosphate + H2O
?
show the reaction diagram
O86025
88.6% of the activity with 4-nitrophenyl phosphate
-
-
?
alpha-naphthyl phosphate + H2O
naphthol + phosphate
show the reaction diagram
-
-
-
-
?
alpha-naphthyl phosphate + H2O
naphthol + phosphate
show the reaction diagram
-
-
-
-
?
alpha-naphthyl phosphate + H2O
naphthol + phosphate
show the reaction diagram
-
-
-
-
?
alpha-naphthyl phosphate + H2O
naphthol + phosphate
show the reaction diagram
-
-
-
-
?
alpha-naphthyl phosphate + H2O
naphthol + phosphate
show the reaction diagram
-
-
-
-
?
alpha-naphthyl phosphate + H2O
naphthol + phosphate
show the reaction diagram
-
hydrolyzed by isoenzyme II and III, no activity with isoenzyme I
-
-
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
show the reaction diagram
-
-
-
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
show the reaction diagram
Neurospora crassa, Neurospora crassa St. L. 74A
-
-
-
?
alpha/beta-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
low activity with alpha-isomer
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
antarctic bacterium
-
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
A1C3J6, -
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
A8TKU6
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
-
alkaline phosphatase F I, alkaline phosphatase F II
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
Q7S2X3
wild-type activity is 9.6% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 18.2fold higher than activity from wild-type enzyme
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
Pasteurella multocida X-73
A1C3J6
-
-
-
?
AMP + H2O
adenosine + phosphate
show the reaction diagram
antarctic bacterium HK47
-
-
-
-
?
arginine phosphate + H2O
Arg + phosphate
show the reaction diagram
-
-
-
-
?
ATP + H2O
?
show the reaction diagram
-
-
-
-
?
ATP + H2O
?
show the reaction diagram
-
-
-
-
?
ATP + H2O
?
show the reaction diagram
-
-
-
-
?
ATP + H2O
?
show the reaction diagram
-
-
-
-
-
ATP + H2O
?
show the reaction diagram
-
-
-
-
?
ATP + H2O
?
show the reaction diagram
-
-
-
-
?
ATP + H2O
?
show the reaction diagram
-
-
-
-
?
ATP + H2O
?
show the reaction diagram
-
-
-
-
?
ATP + H2O
?
show the reaction diagram
-
-
-
-
?
ATP + H2O
?
show the reaction diagram
A1C3J6, -
-
-
-
?
ATP + H2O
?
show the reaction diagram
-
10% of activity with p-nitrophenyl phosphate
-
-
?
ATP + H2O
?
show the reaction diagram
-
alkaline phosphatase F I, alkaline phosphatase F II
-
-
?
ATP + H2O
?
show the reaction diagram
-
57.8% of the activity with 4-nitrophenyl phosphate
-
-
?
ATP + H2O
?
show the reaction diagram
Q7S2X3
wild-type activity is 15.4% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 6.9fold higher than activity from wild-type enzyme
-
-
?
ATP + H2O
?
show the reaction diagram
Porphyromonas gingivalis 381
-
-
-
-
?
ATP + H2O
?
show the reaction diagram
Cobetia marina KMM MC-296
-
10% of activity with p-nitrophenyl phosphate
-
-
?
ATP + H2O
?
show the reaction diagram
Pasteurella multocida X-73
A1C3J6
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
?
ATP + H2O
ADP + phosphate
show the reaction diagram
-
-
-
?
beta-glycerol phosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
A1C3J6, -
-
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
20% of activity with p-nitrophenyl phosphate
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
A1YYW7
uranium precipitation assay: uranyl carbonate solution in carbonate-bicarbonate buffer, supplemented with beta-glycerophosphate as the substrate at 30C under static nongrowing conditions in a final volume of 5 ml
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
Cobetia marina KMM MC-296
-
20% of activity with p-nitrophenyl phosphate
-
-
?
beta-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
Pasteurella multocida X-73
A1C3J6
-
-
-
?
beta-glycerophosphate + H2O
?
show the reaction diagram
-
-
-
-
?
beta-glyceryl phosphate + H2O
glycerol + phosphate
show the reaction diagram
Neurospora crassa, Neurospora crassa St. L. 74A
-
-
-
?
bis(p-nitrophenyl) phosphate + H2O
?
show the reaction diagram
O86025
6.1% of the activity with 4-nitrophenyl phosphate
-
-
?
bis(p-nitrophenyl)phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
bis-4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
show the reaction diagram
A1C3J6, -
-
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
show the reaction diagram
-
weak activity
-
-
?
bis-p-nitrophenyl phosphate + H2O
?
show the reaction diagram
Pasteurella multocida X-73
A1C3J6
-
-
-
?
bromochloroindolyl phosphate + nitroblue tetrazolium
?
show the reaction diagram
-
i.e. BCIP/NBT system
-
?
cAMP + H2O
?
show the reaction diagram
-
-
-
?
casein + H2O
?
show the reaction diagram
-
-
-
-
?
casein + H2O
?
show the reaction diagram
-
enzyme shows protein phosphatase activity
-
?
casein + H2O
?
show the reaction diagram
Porphyromonas gingivalis 381
-
-
-
-
?
casein + H2O
?
show the reaction diagram
Saccharomyces cerevisiae 257
-
enzyme shows protein phosphatase activity
-
?
CMP + H2O
cytidine + phosphate
show the reaction diagram
-
alkaline phosphatase F I, alkaline phosphatase F II
-
-
?
cysteamine S-phosphate + H2O
cysteamine + phosphate
show the reaction diagram
-
-
-
-
?
cytidine 5'-monophosphate + H2O
?
show the reaction diagram
O86025
343.8% of the activity with 4-nitrophenyl phosphate
-
-
?
cytidine phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
D-fructose 1,6-diphosphate + H2O
?
show the reaction diagram
-
52% of the activity with 4-nitrophenyl phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
36% of the activity with 4-nitrophenyl phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
-
5.2% of the activity with 4-nitrophenyl phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
Q7S2X3
wild-type activity is 2.2% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 52fold higher than activity from wild-type enzyme
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
A1C3J6, -
-
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
32% of the activity with 4-nitrophenyl phosphate
-
-
?
D-glucose 1-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
Q7S2X3
wild-type activity is 9.6% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 21fold higher than activity from wild-type enzyme
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
A1C3J6, -
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
19.4% of the activity with 4-nitrophenyl phosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
-
60% of the activity with 4-nitrophenyl phosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
Q7S2X3
wild-type activity is 6.6% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 34.5fold higher than activity from wild-type enzyme
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
Saccharomyces cerevisiae 257
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
-
-
-
-
?
D-ribose 5-phosphate + H2O
D-ribose + phosphate
show the reaction diagram
-
-
-
-
?
dAMP + H2O
?
show the reaction diagram
-
-
-
-
?
dATP + H2O
?
show the reaction diagram
-
-
-
-
?
dCMP + H2O
?
show the reaction diagram
-
-
-
-
?
dCTP + H2O
?
show the reaction diagram
-
-
-
-
?
dentine phosphoprotein + H2O
?
show the reaction diagram
-
-
-
-
?
dGMP + H2O
?
show the reaction diagram
-
-
-
-
?
dGTP + H2O
?
show the reaction diagram
-
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
A1C3J6, -
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
no activity
-
-
-
diphosphate + H2O
2 phosphate
show the reaction diagram
-
weak activity
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
weak activity
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
alkaline phosphatase F I, alkaline phosphatase F II
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
Candida tropicalis CBS 6947
-
-
-
-
?
disodium 3-(4-meth- oxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]- decan]-4-yl)phenyl phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
dTTP + H2O
?
show the reaction diagram
-
-
-
-
?
ethyl phosphate + H2O
ethanol + phosphate
show the reaction diagram
-
-
-
-
?
etoposide phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
fructose 1,6-diphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
fructose 1,6-diphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
fructose 1,6-diphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
gamma-glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
show the reaction diagram
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
show the reaction diagram
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
show the reaction diagram
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
show the reaction diagram
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
show the reaction diagram
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
show the reaction diagram
-
-
-
-
?
glucose 1-phosphate + H2O
glucose + phosphate
show the reaction diagram
-
93% of the activity with 4-nitrophenyl phosphate
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
-
alkaline phosphatase F I, alkaline phosphatase F II
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
Candida tropicalis CBS 6947
-
-
-
-
?
Glucose 6-phosphate + H2O
Glucose + phosphate
show the reaction diagram
Bacillus licheniformis MC14
-
-
-
-
?
glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
-
-
-
?
glycerophosphate + H2O
glycerol + phosphate
show the reaction diagram
-
63% of the activity with 4-nitrophenyl phosphate
-
-
?
glycerophosphate + H2O
?
show the reaction diagram
O86025
248.7% of the activity with 4-nitrophenyl phosphate
-
-
?
glycogen synthase + H2O
?
show the reaction diagram
-
-
-
-
?
GMP + H2O
guanosine + phosphate
show the reaction diagram
-
-
-
-
?
GMP + H2O
guanosine + phosphate
show the reaction diagram
-
alkaline phosphatase F I, alkaline phosphatase F II
-
-
?
GTP + H2O
?
show the reaction diagram
-
-
-
-
?
GTP + H2O
?
show the reaction diagram
antarctic bacterium, antarctic bacterium HK47
-
-
-
-
?
guanosine 5'-monophosphate + H2O
?
show the reaction diagram
O86025
358.8% of the activity with 4-nitrophenyl phosphate
-
-
?
guanosine phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
histidinol phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
histone + H2O
?
show the reaction diagram
-
32P-labelled
-
-
?
histone II-A + H2O
?
show the reaction diagram
-
enzyme shows protein phosphatase activity
-
?
HMG-CoA reductase + H2O
?
show the reaction diagram
-
-
-
-
?
indoxyl phosphate + nitroblue tetrazolium chloride
nitrioblue diformazan + phosphate
show the reaction diagram
-
-
-
?
L-histidinol phosphate + H2O
L-histidinol + phosphate
show the reaction diagram
-
-
-
-
?
L-histidinyl phosphate + H2O
L-histidinol + phosphate
show the reaction diagram
Neurospora crassa, Neurospora crassa St. L. 74A
-
-
-
?
methyl 4-nitrophenyl phosphate + H2O
methyl phosphate + 4-nitrophenol
show the reaction diagram
-
-
-
-
?
methyl 4-nitrophenyl phosphorothioate + H2O
4-nitrophenol + methyl phosphorothioate
show the reaction diagram
-
only the R-enantiomer is detectably hydrolyzed by the enzyme
-
-
?
methyl p-nitrophenyl phosphate + H2O
methanol + p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
methyl p-nitrophenyl phosphorothioate + H2O
methanol + p-nitrophenol + phosphorothioate
show the reaction diagram
-
-
-
-
?
N-acetylcysteamine S-phosphate + H2O
N-acetylcysteamine + phosphate
show the reaction diagram
-
-
-
-
?
NAD+ + H2O
?
show the reaction diagram
-
alkaline phosphatase F I, alkaline phosphatase F II
-
-
?
NADP+ + H2O
?
show the reaction diagram
-
20% of activity with p-nitrophenyl phosphate
-
-
?
NADPH-cytochrome reductase + H2O
?
show the reaction diagram
-
-
-
-
?
o-carboxyphenyl phosphate + H2O
o-carboxyphenol + phosphate
show the reaction diagram
-
-
-
-
?
O-phospho-DL-serine + H2O
DL-serine + phosphate
show the reaction diagram
-
-
-
?
O-phospho-DL-tyrosine + H2O
DL-tyrosine + phosphate
show the reaction diagram
-
-
-
?
O-phosphoserine + H2O
serine + phosphate
show the reaction diagram
-
-
-
?
O-phosphoserine + H2O
serine + phosphate
show the reaction diagram
B4EKR2, -
-
-
-
?
O-phosphoserine + H2O
serine + phosphate
show the reaction diagram
Q7S2X3
wild-type activity is 14.0% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 10.9fold higher than activity from wild-type enzyme
-
-
?
O-phosphothreonine + H2O
threonine + phosphate
show the reaction diagram
-
-
-
?
O-phosphothreonine + H2O
threonine + phosphate
show the reaction diagram
Q7S2X3
wild-type activity is 21.3% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 9.8fold higher than activity from wild-type enzyme
-
-
?
O-phosphotyrosine + H2O
tyrosine + phosphate
show the reaction diagram
-
-
-
?
O-phosphotyrosine + H2O
tyrosine + phosphate
show the reaction diagram
B4EKR2, -
-
-
-
?
O-phosphotyrosine + H2O
tyrosine + phosphate
show the reaction diagram
Q7S2X3
wild-type activity is 68.3% of wild-type activity with 4-nitrophenyl phosphate. Activity with mutant os-1 enzyme is 8.6fold higher than activity from wild-type enzyme
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
P05187
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
antarctic bacterium
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
A1C3J6, -
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
hydrolyzed by isoenzyme I, II or III
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
B4EKR2, -
activities towards tyrosine phosphatase substrate ENCpYINASL and calcineurin substrate DLDVPIPGRDFRRVpSVAAE were also detected, further substrates: ATP, sn-glycerol 3-phosphate
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
Porphyromonas gingivalis 381
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
Pseudomonas aeruginosa H103
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
Pasteurella multocida X-73
A1C3J6
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
antarctic bacterium HK47
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
Synechococcus elongatus PCC 7942 R2
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
Candida tropicalis CBS 6947
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
Bacillus licheniformis MC14
-
-
-
-
?
p-nitrophenyl phosphothioate + H2O
p-nitrophenol + phosphothioate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl sulfate + H2O
p-nitrophenol + sulfate
show the reaction diagram
-
-
-
-
?
p-toluidinium 5-bromo-4-chloro-3-indolyl phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
paraoxon + H2O
?
show the reaction diagram
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
show the reaction diagram
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
show the reaction diagram
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
show the reaction diagram
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
show the reaction diagram
-
-
-
-
?
phenyl phosphate + H2O
phenol + phosphate
show the reaction diagram
-
-
-
-
?
phospho-DL-Thr + H2O
phosphate + Thr
show the reaction diagram
-
-
-
-
?
phospho-DL-Tyr + H2O
phosphate + Tyr
show the reaction diagram
-
-
-
-
?
phospho-Ser histone + H2O
?
show the reaction diagram
-
-
-
-
?
phospho-Ser-casein + H2O
?
show the reaction diagram
-
-
-
-
?
phospho-Tyr angiotensin + H2O
angiotensin + phosphate
show the reaction diagram
-
-
-
-
?
phospho-Tyr-casein + H2O
?
show the reaction diagram
-
-
-
-
?
phospho-Tyr-histone + H2O
?
show the reaction diagram
-
-
-
-
?
phosphocholine + H2O
choline + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + H2O
pyruvate + phosphate
show the reaction diagram
B4EKR2, -
-
-
-
?
phosphoethanolamine + H2O
phosphate + ethanolamine
show the reaction diagram
-
-
-
-
?
phosphoethanolamine + H2O
phosphate + ethanolamine
show the reaction diagram
-
-
-
-
?
phosphoethanolamine + H2O
phosphate + ethanolamine
show the reaction diagram
-
-
-
-
?
phosphoethanolamine + H2O
phosphate + ethanolamine
show the reaction diagram
-
hydrolyzed by isoenzyme III, weak activity with isoenzyme II, no activity with isoenzyme I
-
-
?
phosphorylase kinase + H2O
?
show the reaction diagram
-
-
-
-
?
phosphorylated acetyl-CoA carboxylase + H2O
acetyl-CoA carboxylase + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylcholine + H2O
phosphate + choline
show the reaction diagram
-
-
-
-
?
phosphorylcholine + H2O
phosphate + choline
show the reaction diagram
-
hydrolyzed by isoenzyme III, no activity with isoenzyme I and II
-
-
?
phosphoserine + H2O
phosphate + Ser
show the reaction diagram
-
-
-
-
?
phosphoserine + H2O
phosphate + Ser
show the reaction diagram
-
-
-
-
?
phosphoserine + H2O
phosphate + Ser
show the reaction diagram
-
-
-
-
?
phosphoserine + H2O
phosphate + Ser
show the reaction diagram
-
hydrolyzed by isoenzyme II, weak activity with isoenzyme I and II
-
-
?
phosphoserine + H2O
phosphate + Ser
show the reaction diagram
-
9.3% of the activity with 4-nitrophenyl phosphate
-
-
?
phosphoserine + H2O
phosphate + Ser
show the reaction diagram
Porphyromonas gingivalis 381
-
-
-
-
?
phosphothreonine + H2O
phosphate + Thr
show the reaction diagram
-
22.1% of the activity with 4-nitrophenyl phosphate
-
-
?
phosphotyrosine + H2O
phosphate + Tyr
show the reaction diagram
-
23.7% of the activity with 4-nitrophenyl phosphate
-
-
?
phosvitin + H2O
?
show the reaction diagram
-
-
-
-
?
poly(I) + H2O
?
show the reaction diagram
-
-
-
-
?
polyC + H2O
?
show the reaction diagram
-
-
-
-
?
polymetaphosphate + H2O
?
show the reaction diagram
-
-
-
-
?
polyphosphate PP-25 + H2O
?
show the reaction diagram
-
-
-
-
?
protamine + H2O
?
show the reaction diagram
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
?
show the reaction diagram
Porphyromonas gingivalis 381
-
-
-
-
?
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
show the reaction diagram
-
-
-
?
Raytide + H2O
?
show the reaction diagram
-
-
-
-
?
riboflavin 5'-phosphate + H2O
riboflavin + phosphate
show the reaction diagram
-
-
-
-
?
S-(carboxymethyl)phosphorothioate + H2O
?
show the reaction diagram
-
-
-
-
?
S-[2-(methoxy carbonyl)ethyl] phosphorothioate + H2O
?
show the reaction diagram
-
-
-
-
?
spermidine N'-acetyltransferase + H2O
?
show the reaction diagram
-
-
-
-
?
thiamin diphosphate + H2O
thiamin phosphate + phosphate
show the reaction diagram
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
show the reaction diagram
-
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
-
-
-
?
triphosphate + H2O
diphosphate + phosphate
show the reaction diagram
-
-
-
-
?
tyrosine phosphate + H2O
tyrosine + phosphate
show the reaction diagram
Chenopodium rubrum
-
-
-
-
?
UDP + H2O
?
show the reaction diagram
-
-
-
-
?
UDP + H2O
?
show the reaction diagram
-
-
-
-
?
UDP-glucose + H2O
?
show the reaction diagram
-
20% of activity with p-nitrophenyl phosphate
-
-
?
UMP + H2O
uridine + phosphate
show the reaction diagram
-
-
-
-
?
UMP + H2O
uridine + phosphate
show the reaction diagram
-
alkaline phosphatase F I, alkaline phosphatase F II
-
-
?
uridine 5'-monophosphate + H2O
?
show the reaction diagram
O86025
388.6% of the activity with 4-nitrophenyl phosphate
-
-
?
uridine phosphate + H2O
?
show the reaction diagram
-
-
-
-
?
UTP + H2O
?
show the reaction diagram
-
-
-
-
?
UTP + H2O
?
show the reaction diagram
antarctic bacterium
-
-
-
-
?
UTP + H2O
?
show the reaction diagram
-
67% of the activity with 4-nitrophenyl phosphate
-
-
?
UTP + H2O
?
show the reaction diagram
antarctic bacterium HK47
-
-
-
-
?
methyl phosphate + H2O
methanol + phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme with limited substrate specificity, no dephosphorylation of ATP, PEP, glucose 6-phosphate, phosphoinositol 4',5'-bisphosphate, phosphoproteins
-
-
-
additional information
?
-
-
non-specific enzyme, wide substrate specificity, no phosphate transfer with alcohols, except for Tris
-
?
additional information
?
-
-
the enzyme also catalyses the transfer of the phosphoryl group to alcohols
-
?
additional information
?
-
-, Q9UZV2
the enzyme also dephosphorylizes cohesive and blunt ends of DNA fragments, cohesive ends are slightly preferred
-
?
additional information
?
-
-
the enzyme is a nonspecific phosphomonoesterase that functions through a phosphoseryl intermediate to produce free inorganic phosphate or to transfer the phosphoryl group to other alcohols
-
?
additional information
?
-
-
the enzyme is involved in the biochemical amplification process of excitation or adaption
-
-
-
additional information
?
-
-
involvement of the enzyme in sugar metabolism
-
-
-
additional information
?
-
-
alkaline phosphatase activity is decreased during vitamin C deficiency. The decreased expression of collagen, alkaline phosphatase, and osteocalcin can explain the defects in bone caused by scurvy
-
-
-
additional information
?
-
-
enzyme is important in bone formation and mineralization
-
?
additional information
?
-
-
enzyme is impportant in bone formation and mineralization
-
?
additional information
?
-
-
the enzyme is involved in recovering of phosphate esters when free phosphate is depleted
-
?
additional information
?
-
-
the enzyme is involved in the regulation of mineralization of cartilage matrix
-
?
additional information
?
-
-
the enzyme is necessary for the initiation of mineralization by osteoblast-derived matrix vesicles but not for the continuation of the processes
-
?
additional information
?
-
-
a low level of high-molecular weight alkaline phosphatase is produced constitutively, low-molecular weight alkaline phosphatase is produced only after induction
-
-
-
additional information
?
-
-
important enzyme in the final stages of cell division when Pseudomonas aeruginosa is cultured in inorganic phosphate-limiting media
-
-
-
additional information
?
-
-
high-molecular weight alkaline phosphatase is active as phosphomonoesterase, low-molecular weight alkaline phosphatase is active as phosphomonoesterase and phosphodiesterase
-
-
-
additional information
?
-
-
could be a component of muscle regulatory mechanism at the biochemical level secondary to hyper-regulation of Chasmagnathus granulatus
-
-
-
additional information
?
-
-
HcALP is a Cry1Ac binding protein
-
-
-
additional information
?
-
-
hypophosphatasia is an inherited disorder caused by mutations in the bone alkaline phosphatase gene
-
-
-
additional information
?
-
-
hypophosphatasia is caused by deficiency of activity of the tissue-nonspecific alkaline phosphatase, resulting in a defect of bone mineralization
-
-
-
additional information
?
-
-
levamisole-insensitive alkaline phosphatase activity could be a component of muscle regulatory mechanism at the biochemical level secondary to hyper-regulation of Chasmagnathus granulatus
-
-
-
additional information
?
-
-
motion required for the formation of the enzyme-phosphate complex is minimal on the part of alkaline phosphatase
-
-
-
additional information
?
-
-
the enzyme catalyzes the oxidation of phosphite to phosphate and molecular H2: H2PO3 + H2O = H3PO4 + H2
-
-
-
additional information
?
-
-
involvement of androgen receptor positive chondrocytes in thyroid cartilage mineralization, probably by a testosterone-linked stimulation of alkaline phosphatase
-
-
-
additional information
?
-
-
strong correlations between ALP activity and lipid accumulation. These data suggest that ALP and fat storage are tightly linked during preadipocyte maturation
-
-
-
additional information
?
-
-
the product of the PHO8 gene is repressible by phosphate in the medium
-
-
-
additional information
?
-
Q7S2X3
no hydrolysis of diphosphate
-
-
-
additional information
?
-
-
the purified alkaline phosphatase removes the 5'-phosphate group of a linearized plasmid without showing DNAase activity
-
-
-
additional information
?
-
-
TNAP is an essential component of serum calcification activity and that its role in the shotgun mechanism is to activate the serum nucleator of apatite crystal formation
-
-
-
additional information
?
-
A3ZF85, -
enzmye exclusively phosphomonoesters as a substrate, and not phosphodiesters
-
-
-
additional information
?
-
-
IAP possesses lipopolysaccaride-dephosphorylating activity
-
-
-
additional information
?
-
Pseudomonas aeruginosa H103
-
a low level of high-molecular weight alkaline phosphatase is produced constitutively, low-molecular weight alkaline phosphatase is produced only after induction, high-molecular weight alkaline phosphatase is active as phosphomonoesterase, low-molecular weight alkaline phosphatase is active as phosphomonoesterase and phosphodiesterase
-
-
-
additional information
?
-
Saccharomyces cerevisiae 257
-
non-specific enzyme, wide substrate specificity, no phosphate transfer with alcohols, except for Tris
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pyridoxal 5'-phosphate + H2O
pyridoxal + phosphate
show the reaction diagram
-
-
-
?
diphosphate + H2O
2 phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
-
the enzyme is involved in the biochemical amplification process of excitation or adaption
-
-
-
additional information
?
-
-
involvement of the enzyme in sugar metabolism
-
-
-
additional information
?
-
-
alkaline phosphatase activity is decreased during vitamin C deficiency. The decreased expression of collagen, alkaline phosphatase, and osteocalcin can explain the defects in bone caused by scurvy
-
-
-
additional information
?
-
-
enzyme is important in bone formation and mineralization
-
?
additional information
?
-
-
enzyme is impportant in bone formation and mineralization
-
?
additional information
?
-
-
the enzyme is involved in recovering of phosphate esters when free phosphate is depleted
-
?
additional information
?
-
-
the enzyme is involved in the regulation of mineralization of cartilage matrix
-
?
additional information
?
-
-
the enzyme is necessary for the initiation of mineralization by osteoblast-derived matrix vesicles but not for the continuation of the processes
-
?
additional information
?
-
-
a low level of high-molecular weight alkaline phosphatase is produced constitutively, low-molecular weight alkaline phosphatase is produced only after induction
-
-
-
additional information
?
-
-
important enzyme in the final stages of cell division when Pseudomonas aeruginosa is cultured in inorganic phosphate-limiting media
-
-
-
additional information
?
-
-
could be a component of muscle regulatory mechanism at the biochemical level secondary to hyper-regulation of Chasmagnathus granulatus
-
-
-
additional information
?
-
-
HcALP is a Cry1Ac binding protein
-
-
-
additional information
?
-
-
hypophosphatasia is an inherited disorder caused by mutations in the bone alkaline phosphatase gene
-
-
-
additional information
?
-
-
hypophosphatasia is caused by deficiency of activity of the tissue-nonspecific alkaline phosphatase, resulting in a defect of bone mineralization
-
-
-
additional information
?
-
-
levamisole-insensitive alkaline phosphatase activity could be a component of muscle regulatory mechanism at the biochemical level secondary to hyper-regulation of Chasmagnathus granulatus
-
-
-
additional information
?
-
-
involvement of androgen receptor positive chondrocytes in thyroid cartilage mineralization, probably by a testosterone-linked stimulation of alkaline phosphatase
-
-
-
additional information
?
-
-
strong correlations between ALP activity and lipid accumulation. These data suggest that ALP and fat storage are tightly linked during preadipocyte maturation
-
-
-
additional information
?
-
-
the product of the PHO8 gene is repressible by phosphate in the medium
-
-
-
additional information
?
-
-
TNAP is an essential component of serum calcification activity and that its role in the shotgun mechanism is to activate the serum nucleator of apatite crystal formation
-
-
-
additional information
?
-
Pseudomonas aeruginosa H103
-
a low level of high-molecular weight alkaline phosphatase is produced constitutively, low-molecular weight alkaline phosphatase is produced only after induction
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Al3+
-
activates only the extracellular form
Al3+
-
inhibits high molecular weight and low molecular weight alkaline phosphatase non-competitively
Al3+
C1K6P2
inhibitory effect
Ba2+
-
2 mM, 2.2fold increase in activity
BaCl2
-
10 mM, 3.4fold increase in activity
Ca2+
-
2 mM, 4.95fold increase in activity
Ca2+
A1C3J6, -
activates. D527 of PhoX might be the ligand bound to the catalytic calcium
Ca2+
A3ZF85, -
required for activity
Ca2+
-
partly restores enzymatic activity after EDTA treatment. When Mg2+ is combined with Zn2+, it enhances the catalytic activity up to 3fold
Ca2+
-
activates isoenzyme I, weak activation of isoenzyme III
Ca2+
-
20-25% stimulation
Ca2+
-
activates
CaCl2
-
1 mM, 1.6fold increase in activity
Cd2+
C1K6P2
inhibitory effect
Co2+
-
required
Co2+
-
metalloenzyme, dependent on, can partially be substituted by Mg2+ and Mn2+
Co2+
-
activity is dependent on metal ion, Co2+ is the most active stimulator and has unique effect at high temperature
Co2+
Q153J0
0.1 mM, 2.4fold increase in activity
Co2+
-
2 mM, 2.6fold increase in activity
Co2+
Q7S2X3
26% stimulation of hydrolysis of 4-nitrophenyl phosphate. KM: 0.0022 mM for wild-type enzyme, 0.00051 mM for mutant os-1 enzyme
Co2+
O86025
1 mM, activates
Co2+
A8WEG4, -
a divalent cation is essential, with a combination of Mg2+ and Co2+ or Zn2+ preferred
Co2+
-
enzyme exhibits 1.4fold activation in the presenece of 1 mM Co2+
Co2+
-
50fold increase in activity compared with activity before EDTA treatment
Co2+
-
enhances activity, twice as active than with either Zn2+ or Mn2+
Co2+
-
no stimulation
Fe2+
Q153J0
0.1 mM, 1.25fold increase in activity
Fe2+
-
2 mM, 2.8fold increase in activity
Fe3+
B4EKR2, -
Fe(III) and Zn(II) binuclear centre
Hg2+
C1K6P2
inhibitory effect
K+
-
0.1 M, stimulates
KCl
-
enzyme exhibits highest activity in presence of 100 mM KCl
Magnesium
-
enzyme contains magnesium
Mg2+
-
activation
Mg2+
P05187
metalloenzyme, metal binding site structure
Mg2+
shrimp
-
metalloenzyme, 1 magnesium ion per monomer, binding structure
Mg2+
-
enzyme contains 1 Mg2+ ion per monomer, located near the active site, interacting with phosphate
Mg2+
-
metalloenzyme, can partially substitute for Co2+
Mg2+
-
2fold activation at 10 mM, dependent on, if 4-nitrophenyl phosphate is used as a substrate, protein phosphatase activity is not Mg2+-dependent
Mg2+
-
activity is dependent on metal ion, Co2+, Mg2+ and Zn2+ are the main activators
Mg2+
-
metalloprotein contains Zn2+ and Mg2+, both of which are necessary for catalytic function
Mg2+
Halomonas sp.
-
2 mM, 2.1fold stimulation
Mg2+
-
activity is greatly enhanced by simultaneous addition of Mg2+ and Zn2+. Maximal specific activity in presence of 20 mM MgCl2 and 5 mM ZnCl2
Mg2+
-
activates alkaline phosphatase F I; activates alkaline phosphatase F II
Mg2+
Q153J0
0.1 mM, 1.3fold increase in activity. 2 mM, 1.6fold increase in activity
Mg2+
-
2 mM, 4.3fold increase in activity
Mg2+
-
wild-type enzyme most likely has one Mg2+ in the active site in addition to three Mg2+ that bind elsewhere. At 18C with 10 mM Mg2+, the enzyme activity is completely stable over 160 min. With no Mg2+ in solution, the activity drops to 20% of the initial activity after 160 min
Mg2+
Q7S2X3
80% stimulation of hydrolysis of 4-nitrophenyl phosphate. KM: 0.0036 mM for wild-type enzyme, 0.0084 mM for mutant os-1 enzyme
Mg2+
-
10 mM MgSO4, activity is enhanced to 239% of control
Mg2+
O86025
1 mM, 10fold activation
Mg2+
A8WEG4, -
a divalent cation is essential, with a combination of Mg2+ and Co2+ or Zn2+ preferred
Mg2+
-
requires Mg2+
Mg2+
-
-
Mg2+
-
stimulates activity of extra- and intracellular form
Mg2+
-
removal of a third metal ion site near the bimetallo site, containing Mg2+, suggests that the Mg2+ ion participates in general base catalysis. Mg2+ ion stabilizes the transferred phosphoryl group in the transition state, and this interaction is distinct from those mediated by the Zn2+ bimetallo site. Positioning of charged or polar groups to interact with all three nonbridging oxygen atoms of the transferred phosphoryl group is important for catalysis of phosphate monoester hydrolysis
Mg2+
-
metalloenzyme containing Mg2+ and Zn2+ with a molar ratio of 1:2, enzyme exhibits 1.6fold activation in the presenece of 1 mM Co2+
Mg2+
-
partly restores enzymatic activity after EDTA treatment. When Mg2+ is combined with Zn2+, it enhances the catalytic activity up to 3fold
Mg2+
-
stimulates glycogen synthase phosphatase activity
Mg2+
-
non-essential mixed-type activator, half-maximal effect at 0.007 mM
Mg2+
-
5 mM, 30-44% stimulation
Mg2+
-
activates
Mg2+
-
strongly activates hydrolysis of p-nitrophenyl phosphate
Mg2+
-
MgCl2, stimulates slightly
Mg2+
-
isoenzyme C1, C2, and B2 contain 6 gatoms of Zn per dimer, removal results in loss of activity
Mg2+
-
stimulates
Mg2+
-
activation of isoenzyme II and III
Mg2+
-
stimulates, required for maintenance of activity at high concentrations of Na+
Mg2+
-
bivalent metal ions required, maximal enhancement in presence of Mg2+
Mg2+
-
20-25% stimulation
Mg2+
-
enhances activity to a lesser extent than Mg2+
Mg2+
-
activates
MgCl2
-
10 mM, 2.1fold increase in activity
Mn2+
-
metalloenzyme, can partially substitute for Co2+
Mn2+
Halomonas sp.
-
2 mM, 1.7fold stimulation
Mn2+
-
activates alkaline phosphatase F I; activates alkaline phosphatase F II
Mn2+
Q153J0
0.1 mM, 1.3fold increase in activity
Mn2+
O86025
1 mM, slight activation
Mn2+
-
stimulates activity of extra- and intracellular form
Mn2+
-
fully restores enzymatic activity after EDTA treatment
Mn2+
-
stimulates glycogen synthase phosphatase activity
Mn2+
-
enhances activity
Mn2+
-
no stimulation
Na+
-
slight activation at 10 mM
Na+
-
0.1 M, stimulates
Na+
-
stimulates activity of extra- and intracellular form
Na+
Halomonas sp.
-
gel filtration fraction is converted to the native structure by Na2SO4 suggesting the importance of Na ion
NaCl
-
10 mM, activity is enhanced to 151% of control
NaCl
B0R9W3, -
assays at 4 M NaCl
Ni2+
-
2 mM, 1-3fold increase in activity
Ni2+
Q7S2X3
23% stimulation of hydrolysis of 4-nitrophenyl phosphate. KM: 0.0019 mM for wild-type enzyme, 0.0037 mM for mutant os-1 enzyme
Ni2+
-
partly restores enzymatic activity after EDTA treatment
phosphate
-
enzyme contains one or two phosphate ions
Sr2+
-
2 mM, 4fold increase in activity
sulfate
-
the rate of irreversible thermal inactivation is strongly reduced by addition of kosmotropic anions like sulfate (half-life increases from 8 to 580 min at 60 C)
Zinc
-
enzyme contains zinc
Zn
-
enzyme contains Zn
Zn
-
contains 2 Zn per dimer; enzyme contains Zn
Zn
-
enzyme contains Zn; enzyme from intestine and kidney contains 4 Zn per dimer
Zn
-
enzyme contains Zn
Zn
-
enzyme contains Zn; enzyme from placenta conains 2-3 Zn per dimer
Zn
Micrococcus sodonensis, Rattus norvegicus
-
enzyme contains Zn
Zn
-
required
Zn
-
one molecule of enzyme contains 2 atoms of zinc
Zn2+
-
activation
Zn2+
P05187
metalloenzyme, metal binding site structure
Zn2+
-
metalloenzyme, mutant T59A contains sn amount similar to the wild-type enzyme, while mutant T59R has almost undetectable amounts of bound metal
Zn2+
shrimp
-
metalloenzyme, 2 zinc ions per monomer, binding structure
Zn2+
-
metalloenzyme
Zn2+
-
enzyme contains 2 Zn2+ ions per monomer, located near the active site, interacting with phosphate
Zn2+
-
can partly substitute for Co2+
Zn2+
-
metalloenzyme, 0.3 mol zinc per mol of monomer, binding structure
Zn2+
-
inhibition at 10 mM, activation at 1 mM
Zn2+
-
activity is dependent on metal ion, Co2+, Mg2+ and Zn2+ are the main activators
Zn2+
-
1 mM, 13% activation
Zn2+
-
metalloprotein contains Zn2+ and Mg2+, both of which are necessary for catalytic function
Zn2+
-
activity is greatly enhanced by simultaneous addition of Mg2+ and Zn2+. Maximal specific activity in presence of 20 mM MgCl2 and 5 mM ZnCl2
Zn2+
-
activates alkaline phosphatase F I; activates alkaline phosphatase F II
Zn2+
-
the enzyme employs a binuclear metallocenter of two Zn2+ ions approximately 4 A apart to facilitate catalysis of phosphate monoester hydrolysis. Alkaline phosphatase catalysis is ultrasensitive to charge sequestered between the active site zinc ions
Zn2+
-
2 mM, 2.1fold increase in activity
Zn2+
-
wild-type enzyme most likely has two Zn2+. Zn2+ release from the active site coincides with total protein structure unfolding
Zn2+
-
strong support for a model in which electrostatic interactions between the bimetallo Zn2+ site and a nonbridging phosphate ester oxygen atom make a significant contribution to the large rate enhancement observed for alkaline phosphatase-catalyzed phosphate monoester hydrolysis
Zn2+
O86025
1 mM, slight activation
Zn2+
A8WEG4, -
a divalent cation is essential, with a combination of Mg2+ and Co2+ or Zn2+ preferred
Zn2+
-
stimulates activity of extra- and intracellular form
Zn2+
-
removal of a third metal ion site near the bimetallo site, containing Mg2+, suggests that the Mg2+ ion participates in general base catalysis. Mg2+ ion stabilizes the transferred phosphoryl group in the transition state, and this interaction is distinct from those mediated by the Zn2+ bimetallo site. Positioning of charged or polar groups to interact with all three nonbridging oxygen atoms of the transferred phosphoryl group is important for catalysis of phosphate monoester hydrolysis
Zn2+
B4EKR2, -
Fe(III) and Zn(II) binuclear centre
Zn2+
-
metalloenzyme containing Mg2+ and Zn2+ with a molar ratio of 1:2
Zn2+
-
fully restores enzymatic activity after EDTA treatment
Zn2+
-
calf enzyme contains 0.2% Zn2+
Zn2+
-
the enzyme contains 0.15% Zn2+
Zn2+
-
required for activity
Zn2+
-
Zn2+-metalloenzyme
Zn2+
-
enhances activity
Zn2+
-
enhances activity to a lesser extent than Mg2+
MnCl2
-
10 mM, activity is enhanced to 138% of control
additional information
Q9UZV2
highly dependent on divalent cations
additional information
-
metalloenzyme
additional information
-
not affected by monovalent cations
additional information
-
effect of metal ions, overview
additional information
-
not affected by F- at 10 mM, protein phosphatase activity is not Mg2+-dependent
additional information
Halomonas sp.
-
optimal activity in absence of NaCl
additional information
-
the SWISS-MODEL program is used to construct a model of isoenzyme rIAP-I. Analysis of the active site of the enzyme and the effect of various combinations of metals at the active site. The model shows the possibility of a Zn triad at the metal-binding position of the active site in rIAP-I; the SWISS-MODEL program is used to construct a model of isoenzyme rIAP-II. Analysis of the active site of the enzyme and the effect of various combinations of metals at the active site
additional information
-
metalloenzyme
additional information
-
each subunit contains an active centre with three distinct metal binding sites and one phosphorylatable Ser
additional information
-
three metal binding sites
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2Z)-2-(benzoylamino)-3-[2-[4-(trifluoromethyl)phenyl]-1-benzothiophen-3-yl]prop-2-enoate
-
with 0.1 mM 35% remaining activity
(4-methoxyphenyl)[2-(4-methoxyphenyl)-1-benzothiophen-3-yl]methanone
-
with 0.1 mM 70% remaining activity
-
1,10-phenanthroline
-
1 mM, irreversibly inactivates the enzyme
1,4-dimethoxy-2-methylbenzene
-
-
-
1-(2-phenyl-1-benzothiophen-3-yl)methanamine
-
with 0.4 mM 76% remaining activity
-
1-(3,4-dihydroxyphenyl)-2-(1H-imidazol-1-yl)ethanone
-
-
-
1-(3,4-dihydroxyphenyl)-2-(2-ethyl-1H-imidazol-1-yl)ethanone
-
-
-
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-benzimidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-imidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(2-phenyl-1H-imidazol-1-yl)ethanone
-
-
-
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-imidazol-1-yl)ethanone
-
-
-
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-pyrazol-1-yl)ethanone
-
-
-
1-(3,4-dihydroxyphenyl)-2-(4H-1,2,4-triazol-4-yl)ethanone
-
-
-
1-(3,4-dihydroxyphenyl)-2-(5,6-dimethyl-1H-benzimidazol-1-yl)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-(propan-2-ylamino)ethanone
-
-
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
-
-
-
1-(3,4-dihydroxyphenyl)-2-[(4-methyl-5-phenyl-4H-1,2,4-triazol-3-yl)sulfanyl]ethanone
-
-
-
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
-
-
-
1-benzothiophen-3-yl 4-fluorophenyl ether
-
with 0.4 mM 78% remaining activity
-
1-benzothiophen-3-yl(4-methoxyphenyl)methanone
-
with 0.1 mM 40% remaining activity
-
1-benzothiophen-3-yl(phenyl)methanone
-
with 0.1 mM 43% remaining activity
1-bromotetramisole
-
-
1-bromotetramisole
-
-
1-chloro-4-ethoxy-2-methylbenzene
-
-
1-chloro-4-methoxy-2-methylbenzene
-
-
-
1-fluoro-4-methoxybenzene
-
-
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-ethylpiperazine
P09487
-
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-methylpiperazine
P09487
-
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]azepane
P09487
-
2,4,6-Trinitrobenzenesulfonic acid
-
enzyme loses 80% of its initial activity after incubation for 30 min with 1.0 mM 2,4,6-trinitrobenzenesulfonic acid in bicarbonate buffer, pH 9.0 at 25C. Increasing concentration can not result in more loss of activity
2,5-dimethoxy-N-(quinolin-3-yl)benzenesulfonamide
-
-
-
2,5dimethoxy-N-(pyridin-3-yl)benzenesulfonamide
-
-
-
2-(1-benzothiophen-2-yl)aniline
-
with 0.4 mM 70% remaining activity
-
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
2-(1H-benzimidazol-2-ylamino)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
2-(2-chlorophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 63% remaining activity
-
2-(2-methylphenyl)-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 5% remaining activity
-
2-(2-nitrophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.4 mM 78% remaining activity
-
2-(3-chlorophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 62% remaining activity
-
2-(3-formyl-1-benzothiophen-2-yl)benzonitrile
-
with 0.4 mM 79% remaining activity
-
2-(3-methoxy-1-benzothiophen-2-yl)benzonitrile
-
with 0.1 mM 57% remaining activity
-
2-(3-methoxy-1-benzothiophen-2-yl)benzonitrile
-
with 0.4 mM 79% remaining activity
-
2-(3-pyridine)-3-oxime-benzo[b]thiophene
-
with 0.4 mM 71% remaining activity
2-(4-bromo-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
2-(4-bromo-2-methyl-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
2-(4-chlorophenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 9% remaining activity
-
2-(4-chlorophenyl)-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 69% remaining activity
-
2-(4-methoxyphenyl)-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 37% remaining activity
2-(4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]piperazin-1-yl)ethanol
P09487
-
2-(naphthalen-2-yl)-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 18% remaining activity
-
2-(pyridin-3-yl)-1-benzothiophene-3-carbaldehyde
-
with 0.4 mM 79% remaining activity
2-chloro-1,4-dimethoxybenzene
-
-
2-ethoxy-5-methyl-N-(pyridin-3-yl)benzenesulfonamide
-
-
-
2-glycerophosphate
-
-
2-iodo-1-benzothiophene
-
with 0.1 mM 41% remaining activity
-
2-iodo-1-benzothiophene
-
with 0.4 mM 54% remaining activity
-
2-mercaptoethanol
Q9UZV2
68% inhibition at 1 mM, 86% inhibition at 10 mM
2-mercaptoethanol
-
-
2-mercaptoethanol
-
10 mM, 70% decrease in activity
2-mercaptoethanol
-
-
2-methoxy-4-nitro-N-(pyridin-3-yl)benzenesulfonamide
-
-
-
2-methoxy-4-nitro-N-(quinolin-3-yl)benzenesulfonamide
-
-
-
2-methoxy-5-methyl-N-(pyridin-3-yl)benzenesulfonamide
-
-
-
2-methoxy-5-methyl-N-(quinolin-3-yl)benzenesulfonamide
-
-
-
2-phenyl-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 41% remaining activity
2-phenyl-1-benzothiophene-3-carbaldehyde
-
with 0.4 mM 77% remaining activity
2-phenyl-1-benzothiophene-3-carbonitrile
-
with 0.1 mM 76% remaining activity
-
2-phenyl-3-oxime-benzo[b]thiophene
-
with 0.1 mM 1% remaining activity
-
2-phenyl-3-oxime-benzo[b]thiophene
-
with 0.4 mM 68% remaining activity
-
2-phenyl-benzo[b]thiophene-3-carboxylic acid
-
with 0.4 mM 78% remaining activity
-
2-phenylalanine
-
-
2-[3-(2,2,2-trifluoroethyl)-1-benzothiophen-2-yl]benzonitrile
-
with 0.1 mM 70% remaining activity
-
2-[3-(4-chlorophenoxy)-1-benzothiophen-2-yl]benzonitrile
-
with 0.4 mM 79% remaining activity
-
2-[3-(4-fluorophenoxy)-1-benzothiophen-2-yl]benzonitrile
-
with 0.1 mM 66% remaining activity
-
2-[4-(1-benzothiophen-3-yl)piperazin-1-yl]phenol
-
with 0.1 mM 49% remaining activity
-
2-[4-(trifluoromethyl)phenyl]-1-benzothiophene-3-carbaldehyde
-
with 0.1 mM 30% remaining activity
-
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
-
-
-
3-(2,4-dichloro-5-fluorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichloro-5-fluorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichloro-5-fluorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichloro-5-fluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichloro-5-fluorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichlorophenyl)-1H-pyrazole-5-carbohydrazide
P09487
-
3-(2,4-dichlorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichlorophenyl)-N,N-diethyl-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichlorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichlorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichlorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichlorophenyl)-N-(2-methoxyethyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichlorophenyl)-N-(2-methylpropyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichlorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichlorophenyl)-N-(3-methylbutyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-dichlorophenyl)-N-(4-hydroxybutyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(2,4-difluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
P09487
-
3-(3-methoxy-1-benzothiophen-2-yl)pyridine
-
with 0.4 mM 44% remaining activity
-
3-(3-methoxy-1-benzothiophen-2-yl)quinoline
-
with 0.1 mM 64% remaining activity
-
3-(4-fluorophenoxy)-1-benzothiophene 1-oxide
-
with 0.4 mM 79% remaining activity
3-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
3-methoxy-2-(2-methylphenyl)-1-benzothiophene
-
with 0.1 mM 73% remaining activity
3-methoxy-2-(4-methoxyphenyl)-1-benzothiophene
-
with 0.1 mM 78% remaining activity
3-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
-
-
-
4-(1-benzothiophen-3-yloxy)benzaldehyde
-
with 0.1 mM 9% remaining activity
-
4-bromo-2,5-dimethoxy-N-(pyridin-3-yl)benzenesulfonamide
-
-
4-methoxy-1,2-dimethylbenzene
-
-
4-[(1-oxido-1-benzothiophen-3-yl)oxy]benzonitrile
-
with 0.4 mM 67% remaining activity
-
4-[[(4,6-dimethylpyrimidin-2-yl)amino]methyl]benzene-1,2-diol
-
-
4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]morpholine
P09487
-
5-bromo-2-methoxy-N-(quinolin-3-yl)benzenesulfonamide
-
-
5-chloro-2-ethoxy-N-(pyridin-3-yl)benzenesulfonamide
-
-
-
6-(1-benzothiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
-
with 0.4 mM 19% remaining activity
6-(1-benzothiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole
-
with 0.4 mM 11% remaining activity
6-(thiophen-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
6-(thiophen-2-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
6-(thiophen-3-yl)-2,3-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
6-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
-
6-(thiophen-3-yl)imidazo[2,1-b][1,3]thiazole hydrochloride
-
-
8-hydroxyquinoline
-
-
Ag2+
-
1 mM, complete inactivation
alendronate
-
0.01-0.1 mM, coincubation with excess Zn2+ or Mg2+ completely abolish inhibition
arsenate
-
irreversible inhibitor
arsenate
-
1 mM Na2HAsO4, 80% inhibition of isoenzyme I, 22% inhibition of isoenzyme II, 40% inhibition of isoenzyme III
arsenate
-
competitive
arsenate
-
-
aspirin
-
2 mM, 84% inhibition
Ba2+
-
1 mM, 95% inhibition of isoenzyme I
bis(1,1,1-trifluoroacetylacetonato)oxovanadium(IV)
-
-
bis(3-chloroacetylacetonato)oxovanadium(IV)
-
-
bis(3-chloroacetylacetonato)oxovanadium(IV)(4-Mepy)
-
-
bis(3-methylacetylacetonato)oxovanadium(IV)
-
-
bis(acetylacetonato)oxovanadium(IV)
-
-
bis(acetylacetonato)oxovanadium(IV)(4-Mepy)
-
-
bis(benzoylacetonato)oxovanadium(IV)
-
-
Borate
-
1 mM H3BO4, 16% inhibition of isoenzyme I, 13% inhibition of isoenzyme II, 8% inhibition of isoenzyme III
butanol
-
reversible noncompetitive
Ca2+
Q9UZV2
17% inhibition at 1 mM
Ca2+
-
1 mM, 50% inhibition
Ca2+
Q153J0
2 mM, 16% inhibition
Ca2+
-
10 mM, glycogen synthase phosphatase activity
Ca2+
-
in presence of 0.005 mM Mg2+, Ca2+ acts as an uncompetitive inhibitor, at 0.1 mM Mg2+, Ca2+ inhibits non-competitively
Ca2+
-
weak inhibition of isoenzyme II
CaCl2
-
1 mM, 32% inhibition
Caffeine
-
uncompetitive inhibition
Cd2+
-
39% inhibition of the enzyme at 1 mM in the gills, but not in digestive gland
Cd2+
-
1 mM, complete inactivation
Cd2+
-
5 mM, 30% inhibition
CN-
-
complete inhibition at 10 mM
CO2
-
enzyme in buffer can be inactivated by COS treatment at atmospheric pressure, increasing inactivation, when temperature increases from 20C to 50C, 16% loss of activity after 30 min at 20C, 81% loss of activity after 30 min at 50C. Change in activity dependent on CO2 treatment is not observed in raw milk mainly due to strong buffering capacity of milk
Co2+
-
1 mM, 54% inhibition
Co2+
-
5 mM, 60% inhibition
Co2+
Q153J0
2 mM, 25% inhibition
corticosterone
-
5 mM, 90% inhibition of alkaline phosphatase grown in high phosphate medium, no effect is observed with alkaline phosphatase grown in low phosphate medium
corticosterone
-
2 mM, 13% inhibition
Cry1Ac toxin
-
environment friendly insecticidal crystal proteins encoded by the spore-forming bacteria Bacillus thuringiensis. Competitive inhibitor; environment friendly insecticidal crystal proteins encoded by the spore-forming bacteria Bacillus thuringiensis. Competitive inhibitor
-
Cu2+
Q9UZV2
28% inhibition at 1 mM
Cu2+
-
1 mM, 70% inhibition
Cu2+
-
1.0 mM, 82% inhibition, levamisole-insensitive alkaline phosphatase activity; 1.0 mM, almost complete inhibition, levamisole-sensitive alkaline phosphatase activity
Cu2+
-
5 mM, 40% inhibition
Cu2+
Q153J0
2 mM, 29% inhibition
Cu2+
-
2 mM, 21% inhiition
Cu2+
-
1 mM, 87% inhibition of isoenzyme I, 10% inhibition of isoenzyme III
Cu2+
-
weak inhibition
CuCl2
-
10 mM, 24% inhibition
CuSO4
-
10 mM, 71% inhibition
Cys
-
uncompetitive inhibition of phosphatase actvity, mixed-competitive inhibition of inorganic pyrophosphatase activity. Inorganic pyrophosphatase activity is inhibited more than phosphatase activity. Ca2+ and Mg2+ ion concentrations may regulate this inhibition
diethyl-p-nitrophenyl phosphate
-
-
dithiothreitol
-
-
dithiothreitol
-
10 mM, 95% decrease in activity
DTT
Q9UZV2
nearly complete inhibition at 2 mM
EDTA
Q9UZV2
90% inhibition at 1 mM
EDTA
-
inactivation after 1 h at 1 mM
EDTA
-
inactivation of the native, but not of the recombinant enzyme, inhibition of the native enzyme is reversible by divalent metal ions, best effect with Co2+
EDTA
-
90% inhibition at 1 mM and 25C, complete inhibition at 0.1 mM EDTA and 90C
EDTA
-
1 mM, complete inactivation
EDTA
Halomonas sp.
-
5 mM, 70% inhibition
EDTA
-
alkaline phosphatase F I; alkaline phosphatase F II
EDTA
-
IC50: 2.26 mM
EDTA
A1C3J6, -
0.01 mM, complete inhibition. Ca2+ is the best metal ion to reconstitute enzyme activity, followed by Co2+, Ni2+, Mn2+, and Mg2+. Zn2+, in contrast, failed to restore enzyme activity
EDTA
-
10 mM, 71% inhibition
EDTA
O86025
-
EDTA
A8WEG4, -
10 mM, 99% inhibition
EDTA
-
completely deactivates the enzyme
EDTA
Bacillus sp. OK-1
-
1 mM, 83% inhibition
EDTA
-
inhibition of isoenzyme I and II
EDTA
-
inhibition is reversed by divalent cations
EDTA
-
reversed by zinc
EDTA
-
optimal reactivation by Zn2+ or Co2+. The Zn2+-reactivated enzyme is stable, the Co2+-apoenzyme is not
EDTA
antarctic bacterium
-
0.1 mM, 50% inhibition
EGTA
Q9UZV2
82% inhibition at 1 mM
ethanol
-
reversible noncompetitive
ethylene glycol
-
reversible noncompetitive
F-
-
50 mM KF, 13% inhibition of p-nitrophenyl phosphate hydrolysis, 50% inhibition of dephosphorylation of P-labelled histones
F-
-
1 mM NaF, 74% inhibition of isoenzyme I, 15% inhibition of isoenzyme II
Fe2+
Q153J0
2 mM, 89% inhibition
-
Fe3+
-
-
-
Glutaraldehyde
-
1%, 65% inactivation
glutathione
-
strong
glycerol
-
concentrations of 10%, 20% and 40% inhibit the activity by 35%, 60%, and 90%
glycerol phosphate
-
-
glycyl-glycine
-
-
Glycyl-leucine
-
-
guanidine hydrochloride
-
inactivation of the enzyme by GuHCl (guanidine hydrochloride) is a slow, reversible reaction with fractional remaining activity. The microscopic rate constants are determined. The enzyme is protected by the substrate to a certain extent during guanidine denaturation. The changes of conformation of the enzyme in different concentrations of GuHCl are studied. The inactivation occurs before the noticeable conformational changes of the enzyme molecule as a whole can be detected, which suggests that the active site of the enzyme has more flexibility than the whole enzyme molecule
heparin
-
histone phosphatase activity
Hg2+
-
1 mM, complete inactivation
Hg2+
-
1 mM nearly complete inhibition of isoenzyme I, II and III
Hg2+
-
1 mM, 82% loss of activity
HgCl2
-
alkaline phosphatase F I; alkaline phosphatase F II
HgCl2
-
10 mM, 74%inhibition
HPO42-
-
competitive
imidazole
-
uncompetitive inhibition
Inorganic phosphate
A8WEG4, -
-
-
Inorganic phosphate
-
-
-
isatin
-
uncompetitive
KCl
Q9UZV2
90% remaining activity
KCl
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
KNO3
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
KPF6
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
-
L-amino acids
P05187
specific uncompetitive inhibition, molecular mechanism involves Arg166 and Glu429
L-Homoarginine
-
83% inhibition at 10 mM for all three isozymes
L-Homoarginine
-
inhibition of an isozyme from the lower part of intestine
L-Homoarginine
-
high sensitivity of the liver/bone/kidney isoenzyme
L-Homoarginine
-
powerful inhibitor of the bone/liver/kidney isoenzyme and for the osteosarcoma cell enzyme
L-Homoarginine
-
marked inhibition of the liver enzyme at concentrations which produce only slight inhibition of placental enzyme
L-Homoarginine
-
-
L-Homoarginine
-
-
L-leucine
-
allozyme D is highly sensitive and shows uncompetitive inhibition, allozymes S and F are less sensitive, allozymes SD and FD, mixed type, respond in an intermediate fashion to inhibition
L-leucine
-
uncompetitive inhibition
L-Phe
-
1 mM, 13% inhibition
L-Phe
-
maximal ainhibition at 1 mM. D-Phe has no effect
L-Phe
-
mixed-type inhibition
L-Phe-Gly-Gly
-
high sensitivity of the intestinal and placental isoenzyme
L-Phe-Gly-Gly
-
marked inhibition of the placental enzyme at concentrations which produce only slight inhibition of liver enzyme
L-Phe-Gly-Gly
-
-
L-phenylalanine
-
uncompetitive inhibition
L-phenylalanine
P08289
10 mM, 100% inhibition; 10 mM, 100% inhibition; 10 mM, 37% inhibition; 10 mM, 37% inhibition, bone isoenzyme; 10 mM, 62% inhibition, isoenzyme rTI2A; 10 mM, 70% inhibition, isoenzyme rTI2B
L-phenylalanine
-
2 mM, 24% inhibition
lansoprazole
-
uncompetitive
lectin
P08289
5 g/L, precipitation by lectin: 100%; 5 g/L, precipitation by lectin: 100%; 5 g/L, precipitation by lectin: 100%, bone isoenzyme; 5 g/L, precipitation by lectin: 58%, isoenzyme rTI2B; 5 g/L, precipitation by lectin: 76%, isoenzyme rTI2A
-
Leu
-
L-Leu, uncompetitive, D-Leu with greatly decreased efficiencies
leucinamide
-
-
leucinol
-
-
levamisole
-
96-98% inhibition at 1 mM for all three isozymes
levamisole
-
-
levamisole
-
complete inhibition of the seminal plasma enzyme at 4.2 mM
levamisole
-
inhibits brush border membrane enzyme activity in the upper villus but is less effective in the middle villus and has no effect on alkaline phosphatase activity in the mucus gel
levamisole
-
0.5 mM, 91% inhibition
levamisole
-
hydrolysis of pyrophosphate by rat aortic rings is inhibited about half by the nonspecific alkaline phosphatase inhibitor levamisole. Hydrolysis is increased in aortic rings from uremic rats and all of this increase is inhibited by levamisole
levamisole
-
with 0.4 mM 10% remaining activity
levamisole
-
-
levamisole
-
10 mM, 94% inhibition of p-nitrophenyl phosphate hydrolysis, 82% inhibition of dephosphorylation of P-labelled histones
levamisole
-
-
levamisole
-
noncompetitive
levamisole
-
-
methyl (2E)-2-(benzoylamino)-3-[2-(4-methoxyphenyl)-1-benzothiophen-3-yl]prop-2-enoate
-
with 0.1 mM 77% remaining activity
methyl 3-(1-benzothiophen-3-yl)-N-benzoylalaninate
-
with 0.4 mM 74% remaining activity
methyl N-benzoyl-3-[2-[4-(trifluoromethyl)phenyl]-1-benzothiophen-3-yl]alaninate
-
with 0.1 mM 63% remaining activity
Mg2+
-
1 mM, 19% inhibition
Mg2+
-
weak inhibition of isoenzyme I
Mn2+
-
1 mM, 43% inhibition
Mn2+
Q153J0
2 mM, 32% inhibition
Mn2+
-
2 mM, 24% inhiition
Mn2+
-
1 mM 90% inhibition of isoenzyme I, 64% inhibition of isoenzyme II, 39% inhibition of isoenzyme III
MnO4-
-
competitive inhibition
Mo2+
-
1 mM, 50% inhibition
molybdate
Q9UZV2
slight inhibition at 10 mM
molybdate
Chenopodium rubrum
-
10 mM, activity of heat-shocked induced phosphatase: -33%
molybdate
-
competitive
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
P09487
-
N-(2-hydroxyethyl)-3-(2,4,5-trifluorophenyl)-1H-pyrazole-5-carboxamide
P09487
-
N-tert-butyl-3-(2,4-dichlorophenyl)-1H-pyrazole-5-carboxamide
P09487
-
Na2SO4
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
Na2[W2O3(O2)4(glycyl-glycine)2](3H2O)
-
-
Na2[W2O3(O2)4(glycyl-leucine)2](3H2O)
-
-
NaBF4
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
-
NaCl
Q9UZV2
2 M, 60% remaining activity
NaCl
-
1 M, inhibition of enzyme form CAPase
NaCl
Halomonas sp.
-
2.0 M, 71% loss of activity
NaCl
-
200 mM, 30% inhibition
NaCl
-
reduces enzymatic activity and significantly decreased Vmax/Km ratio
NaF
-
alkaline phosphatase F I; alkaline phosphatase F II
NaNO3
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
NaWO4
-
1 mM NaWO4, 35% inhibition of isoenzyme I, 80% inhibition of isoenzyme II, 14% inhibition of isoenzyme III
Na[VO(O2)2(asparagine)]H2O
-
-
Na[VO(O2)2(glutamine)]H2O
-
-
Na[VO(O2)2(glycyl-glycine)(H2O)]H2O
-
-
Na[VO(O2)2(triglycine)]3H2O
-
-
NEM
-
very slowly
Ni2+
Q9UZV2
56% inhibition at 1 mM
Ni2+
-
5 mM, 27% inhibition
orthovanadate
-
70% inhibition at 1 mM, competitive
p-chloroanilide phosphonate
-
-
-
p-chloromercuribenzoate
-
0.1-0.2 mM, 85%-100% inhibition
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
reactivation by DTT and 2-mercaptoethanol
p-nitrophenyl phosphorothioate
-
-
pamidronate
-
0.01-0.1 mM, coincubation with excess Zn2+ or Mg2+ completely abolish inhibition
PCMB
-
1 mM, 54% inhibition of isoenzyme I, 33% inhibition of isoenzyme II, 9% inhibition of isoenzyme III
Phe
-
enzyme from intestine is inhibited, enzyme from liver not
Phe
-
20 mM, 82-99% inhibition of the soluble enzyme form, 68-95% inhibition of the particulate enzyme form
Phe
-
marked inhibition of the placental enzyme at concentrations which produce only slight inhibition of liver enzyme
Phe
-
L-Phe, uncompetitive, D-Phe with greatly decreased efficiencies
Phenanthroline
-
-
phenyl phosphonate
-
-
phenyl phosphonate
-
competitive
phenylalanine
-
-
Phenylglyoxal
-
1.0 mM, complete irreversible inactivation after 30 min in bicarbonate buffer, pH 9.0, at 25C
phenylphosphonate
-
10 mM, 47% inhibition of p-nitrophenyl phosphate hydrolysis, 80% inhibition of dephosphorylation of P-labelled histones
phosphate
Q9UZV2
-
phosphate
-
competitive inhibition of both enzyme forms
phosphate
-
competitive inhibition
phosphate
-
competitive inhibition
phosphate
-
conpetitive
phosphate
-
competitive
phosphate
-
-
phosphate
Q7S2X3
-
phosphate
Q17TZ1
competitive inhibitor
phosphate
Chenopodium rubrum
-
2.5 mM, activity of heat-shocked induced phosphatase: -64%
phosphate
-
competitive inhibitor
phosphate
-
competitive inhibitor
phosphate
-
-
phosphate
B0R9W3, -
-
phosphate
-
insensitive
phosphate
-
1 mM Na2HPO4, 74% inhibition of isoenzyme I, 15% inhibition of isoenzyme II, 2% inhibition of isoenzyme III; competitive
phosphate
-
competitive
polylysine
-
histone phosphatase activity
polyphenol-rich beverages
-
21% inhibition
-
progesterone
-
0.5 mM, 29% inhibition
Propanol
-
reversible noncompetitive
protamine
-
histone phosphatase activity
SH-group blocking agents
-
-
-
Sodium acetate
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
Sodium citrate
-
reduced enzymatic activity and significantly decreased Vmax/Km ratio
Sodium deoxycholate
-
1 mM, 20% inhibition
Sodium molybdate
B4EKR2, -
-
Sr2+
-
1 mM, 88% inhibition of isoenzyme I
Tartrate
-
weak inhibition at 10 mM
Tartrate
-
5.9% inhibition at 1 mM
theophylline
-
2 mM, 77% inhibition
theophylline
-
-
theophylline
-
reversible non-competitive inhibitor
thioglycolic acid
-
combined treatment with thioglycolic acid, 0.175%, and 6 M urea leads to reduction of disulfide bonds, loss of activity and separation into subunits
thioglycolic acid
-
-
thiophosphate
-
-
thymidine 5'-O-phosphorothioate
-
-
-
Trimetaphosphate
-
-
-
tungstate
Q17TZ1
competitive inhibitor
tungstate/H2O2
-
-
-
Urea
-
reversible inactivation. At low concentrations of urea, the first detected alteration in properties is an increase in the activity of the enzyme. This is followed by inactivation and the release of half of the zinc content when the amount of urea reaches levels of 2 M. Intrinsic tryptophan fluorescence and circular dichroism ellipticity change in the range 2.5 to 8 M urea, signalling dimer dissociation, followed by one major monomer unfolding transition at 6-8 M urea as indicated by ANS fluorescence and KI fluorescence quenching
Urea
P08289
3 mM, 100% inhibition; 3 mM, 100% inhibition; 3 mM, 68% inhibition, bone isoenzyme; 3 mM, 70% inhibition, isoenzyme rTI2B; 3 mM, 71% inhibition; 3 mM, 80% inhibition, isoenzyme rTI2A
Urea
-
combined treatment with thioglycolic acid, 0.175%, and 6 M urea leads to reduction of disulfide bonds, loss of activity and separation into subunits
uridine 5'-O-phosphorothioate
-
-
vanadate
Q9UZV2
-
vanadate
-
1 mM, 22% inhibition of alkaline phosphatase grown in high phosphate medium
vanadate
Q7S2X3
-
vanadate
A8WEG4, -
10 mM, 89% inhibition
vanadate
-
-
VO3-
-
1 mM, 78% inhibition
WO4 3-
-
competitive inhibition, product analogue
Zn2+
-
about 30% inhibition at 1 mM in gill, mantle, and siphon
Zn2+
-
mutant H412Y in presence of a phosphoryl group acceptor and Zn2+ at 0.1 mM
Zn2+
-
complete inhibition at 15 mM
Zn2+
-
inhibition at 10 mM, activation at 1 mM
Zn2+
Halomonas sp.
-
2 mM, 90% inhibition
Zn2+
-
5 mM, complete inhibition
Zn2+
Q153J0
2 mM, 51% inhibition
Zn2+
-
above 0.02 mM
Zn2+
-
non-competitive inhibition
Zn2+
-
1 mM, 67% inhibition
Zn2+
-
1 mM, 98% inhibition of isoenzyme I
Zn2+
antarctic bacterium
-
-
ZnCl2
-
10 mM, 58% inhibition
ZnCl2
-
1 mM, 16% inhibition
ZnCl2
Chenopodium rubrum
-
0.01 mM, activity of heat-shocked induced phosphatase: -82%
zoledronate
-
0.01-0.1 mM, coincubation with excess Zn2+ or Mg2+ completely abolish inhibition
[WO(O2)2(glycyl-glycine)(H2O)]3H2O
-
-
[WO(O2)2(glycyl-glycine)](3H2O)
-
-
[WO(O2)2(glycyl-leucine)](3H2O)
-
-
[WO(O2)2(triglycine)]3H2O
-
-
additional information
Q9UZV2
no inhibition by molybdate and vanadate
-
additional information
-
no inhibition at 10 mM by L-phenylalanine at 10 mM for all three isozymes
-
additional information
-
tartrate-rsistant
-
additional information
-
inhibition level is tissue-dependent
-
additional information
-
Zn2+ and Mg2+ do not affect the mutant T59R enzyme
-
additional information
-
enzyme is sensitive to environmental salinity
-
additional information
-
iodoacetamide and NaN3 at 2-10 mM concentration have no effect on activity
-
additional information
A8WEG4, -
enzyme is resistant to urea and dithioreitol
-
additional information
-
with increase in concentration of the inhibitor complexes from 0.005 to 0.04 mM, an increase in Km value is observed. Each of the inhibitors serves as a mixed type of inhibitor of ALP, combining competitive and noncompetitive modes of inhibition
-
additional information
-
highly resistant to okadaic acid
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
20-hydroxyecdysone
-
-
Albumin
-
3fold stimulation of hydrophilic enzyme, slight stimulation of amphiphilic enzyme
-
Anions
-
required for maximal activity in the order of decreasing effectiveness: Cl-, Br-, NO3-, ClO4-, SCN-
-
atenolol
-
2 mM, 32% activation
beta-estradiol
-
concentration dependent activation of alkaline phosphatase grown in low phosphate medium
cholesterol
-
concentration dependent activation of alkaline phosphatase grown in low phosphate medium
Co2+
Q9UZV2
2fold activation at 1 mM
corticosterone
-
0.5 mM, 18% activation
diethanolamine
-
highly activates BIALP. Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
EDTA
-
10 mM, 2.7fold increase in activity
insecticide fenvalerate
-
-
-
L-Homoarginine
-
5 mM, activation of alkaline phosphatase grown in high phosphate medium to 186% of the control value, alkaline phosphatase grown in low phosphate medium is activated to 166% of control
L-Leu
-
5 mM, activation of alkaline phosphatase grown in high phosphate medium to 155% of the control value
L-Phe
-
5 mM, activation of alkaline phosphatase grown in high phosphate medium to 168% of the control value
levamisole
-
1 mM, activation of alkaline phosphatase grown in high phosphate medium to 122% of the control value
Mg2+
Q9UZV2
2fold activation at 1 mM
Mg2+
-
95% activation at 1 mM
N-Methylethanolamine
-
highly activates BIALP. Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
NaCl
-
1 M, activation of enzyme form IAPase
NH4Cl
-
10 mM, activity is enhanced to 165% of control
phosphatidylcholine
-
1fold stimulation of hydrophilic enzyme form
phosphatidylethanolamine
-
1fold stimulation of hydrophilic enzyme form
phosphatidylinositol
-
1.5fold stimulation of hydrophilic enzyme form
phosphatidylserine
-
1fold stimulation of amphiphilic enzyme form, 3fold stimulation of hydrophilic enzyme form
progesterone
-
concentration dependent activation of alkaline phosphatase grown in low phosphate medium
propranolol
-
2 mM, 18% activation
simvastatin
-
0.5 mM, 32% activation
triethanolamine
-
highly activates BIALP. Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
Tris
-
activation at 0.2 M, increases with increasing concentration to a plateau
Tris
B0R9W3, -
dephosphorylation of substrate is doubled when the Tris concentration in the reaction buffer is increased from 20 mM to 500 mM
Tris-HCl buffer
-
-
Triton X-100
-
slight activation at 10 mM
Zn2+
Q9UZV2
2fold activation at 1 mM
Zn2+
-
stimulation of mutant enzymes, in presence or absence of a phosphoryl group acceptor in the reaction, except for mutnat H412Y, whose activity is reduced in presence of phosphoryl group acceptor and 0.1 mM Zn2+
additional information
-
Zn2+ and Mg2+ do not affect the mutant T59R enzyme
-
additional information
-
enzyme exhibits highest activity at 50 mM Gly-NaOH
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.5
-
2'-AMP
-
-
0.01
-
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate
-
-
0.085
-
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate
-
-
0.177
-
2-chloro-5-(4-methoxyspiro (1,2-dioxetane-3,2'-(5'-chloro)tricyclo[3.3.1.13,7]decan)-4-yl)phenyl phosphate
-
-
0.026
-
2-naphthyl phosphate
-
purified enzyme
0.078
-
2-naphthyl phosphate
-
membrane-bound enzyme enzyme
2.3
-
3'-AMP
-
-
0.037
-
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
-
layer-by-layer single-stack, immobilized ALP
0.04
-
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
-
direct physical adsorption, immobilized ALP; immobilized ALP
0.05
-
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
-
free ALP
0.1058
-
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
-
layer-by-layer multi-stack, immobilized ALP
0.114
-
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
-
glutaraldehyde X-link DAH, immobilized ALP
1e-08
-
4-nitrophenyl phosphate
-
Vmax (mmol/min mg of protein): 1.8 (dimer), 0.42 (tetramer)
3.5e-07
-
4-nitrophenyl phosphate
-
-
3.5e-07
-
4-nitrophenyl phosphate
Q92058
pH: 8.5
0.00026
-
4-nitrophenyl phosphate
-
-
0.00034
-
4-nitrophenyl phosphate
-
-
0.0035
-
4-nitrophenyl phosphate
-
mutant S105L, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.005
-
4-nitrophenyl phosphate
-
mutant T155M, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.0073
-
4-nitrophenyl phosphate
-
mutant H412Y, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.0073
-
4-nitrophenyl phosphate
-
25C, pH 8, mutant enzyme T81A
0.0078
-
4-nitrophenyl phosphate
-
25C, pH 8, wild-type enzyme
0.0083
-
4-nitrophenyl phosphate
-
IAPase
0.0094
-
4-nitrophenyl phosphate
-
wild-type enzyme, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.0095
-
4-nitrophenyl phosphate
-
mutant E341K, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.0097
-
4-nitrophenyl phosphate
-
mutant S105L, pH 8.0, 25C, in presence of a phosphoryl group acceptor
0.011
-
4-nitrophenyl phosphate
-
mutant E322K, pH 8.0, 25C, in presence of a phosphoryl group acceptor
0.0145
-
4-nitrophenyl phosphate
-
pH 8, 25C, in the presence of phosphate acceptor (1 M Tris-HCl buffer)
0.0156
-
4-nitrophenyl phosphate
-
37C, pH 7.4, 1 mM Ca2+
0.0176
-
4-nitrophenyl phosphate
-
mutant D369N, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.019
-
4-nitrophenyl phosphate
-
37C, pH 7.4, with Ca2+ and Mg2+
0.0211
-
4-nitrophenyl phosphate
-
wild-type enzyme, pH 8.0, 25C, in presence of a phosphoryl group acceptor
0.0218
-
4-nitrophenyl phosphate
-
pH 8.0, 25C, recombinant wild-type enzyme
0.0221
-
4-nitrophenyl phosphate
-
mutant E322K, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.0249
-
4-nitrophenyl phosphate
-
pH 8.0, 25C, recombinant mutant T59A
0.027
-
4-nitrophenyl phosphate
-
37C, pH 7.4, 1 mM Ca2+, 1 mM Mg2+
0.028
-
4-nitrophenyl phosphate
-
isozyme B2, pH 8.8
0.02982
-
4-nitrophenyl phosphate
P00634
single-chain Fv antibody fusion protein
0.0315
-
4-nitrophenyl phosphate
A8WEG4, -
-
0.034
-
4-nitrophenyl phosphate
-
isozyme B1, pH 8.8
0.034
-
4-nitrophenyl phosphate
Q153J0
75C
0.035
-
4-nitrophenyl phosphate
-
37C, pH 7.4, 1 mM Mg2+
0.0374
-
4-nitrophenyl phosphate
-
mutant E341K, pH 8.0, 25C, in presence of a phosphoryl group acceptor
0.038
-
4-nitrophenyl phosphate
-
isozyme B/I, pH 8.8
0.039
-
4-nitrophenyl phosphate
-
25C, pH 8.0, mutant enzyme G51C
0.039
-
4-nitrophenyl phosphate
O86025
80C, pH 12
0.0392
-
4-nitrophenyl phosphate
-
pH 8.0, 25C, recombinant mutant T59R
0.046
-
4-nitrophenyl phosphate
-
25C, pH 8.0, mutant enzyme I50C
0.057
-
4-nitrophenyl phosphate
-
CAPase
0.057
-
4-nitrophenyl phosphate
-
mutant T155M, pH 8.0, 25C, in presence of a phosphoryl group acceptor
0.058
-
4-nitrophenyl phosphate
-
25C, pH 8.0, mutant enzyme S52C
0.059
-
4-nitrophenyl phosphate
-
25C, pH 8.0, mutant enzyme S53C
0.0597
-
4-nitrophenyl phosphate
-
mutant D369N, pH 8.0, 25C, in presence of a phosphoryl group acceptor
0.06
-
4-nitrophenyl phosphate
-
10C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
0.062
-
4-nitrophenyl phosphate
-
pH 9.5, 70C, wild-type enzyme
0.0691
-
4-nitrophenyl phosphate
-
mutant D434E, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.07
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.05 M diethanolamine
0.074
-
4-nitrophenyl phosphate
-
in absence of Mg2+
0.082
-
4-nitrophenyl phosphate
-
pH 9.5, 37C, Vmax: 0.96 nmol/min/mg enzyme, CIAP immobilized enzyme reactor (in excellent agreement with a Km value of calf ALP enzyme using a 96-well microplate reader)
0.087
-
4-nitrophenyl phosphate
C1K6P2
pH 9.5, 50C, Vmax: 0.049 micromol/min/mg
0.09
-
4-nitrophenyl phosphate
-
in presence of Mg2+
0.09
-
4-nitrophenyl phosphate
-
pH 10.5, mutant V406A
0.09
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.05 M methylamine
0.093
-
4-nitrophenyl phosphate
-
pH 8.0, 65C
0.11
-
4-nitrophenyl phosphate
-
allozyme D, pH 9.8, in presence of Mg2+ and Zn2+
0.11
-
4-nitrophenyl phosphate
-
37C, native enzyme
0.11
-
4-nitrophenyl phosphate
-
25C, pH 8.0, wild-.type enzyme
0.12
-
4-nitrophenyl phosphate
-
37C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
0.13
-
4-nitrophenyl phosphate
-
37C, native enzyme
0.16
-
4-nitrophenyl phosphate
-
25C, pH 8, wild-type enzyme
0.17
-
4-nitrophenyl phosphate
-
57C, native enzyme
0.175
-
4-nitrophenyl phosphate
-
pH 8.0, 25C
0.18
-
4-nitrophenyl phosphate
-
57C, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.18
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.2 M N-methylethanolamine
0.198
-
4-nitrophenyl phosphate
-
mutant H412Y, pH 8.0, 25C, in presence of a phosphoryl group acceptor
0.2
-
4-nitrophenyl phosphate
-
37C, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.2
-
4-nitrophenyl phosphate
Q7S2X3
37C, pH 9.5, mutant os-1 enzyme, without MgCl2
0.21
-
4-nitrophenyl phosphate
-
pH 10.5, wild-type
0.22
-
4-nitrophenyl phosphate
-
-
0.22
-
4-nitrophenyl phosphate
-
intracellular form
0.23
-
4-nitrophenyl phosphate
-
37C, native enzyme, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.23
-
4-nitrophenyl phosphate
-
25C, pH 8, mutant enzyme T81A
0.238
-
4-nitrophenyl phosphate
-
pH 7.4, 37C
0.24
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.1 M triethanolamine
0.26
-
4-nitrophenyl phosphate
-
10C, native enzyme
0.27
-
4-nitrophenyl phosphate
Q7S2X3
37C, pH 9.5, wild-type enzyme, without MgCl2
0.27
-
4-nitrophenyl phosphate
-
without Mg2+
0.28
-
4-nitrophenyl phosphate
-
intracellular form
0.3
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.05 M ethanolamine; pH 9.8, 20C, 1 M ethanolamine
0.31
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M triethanolamine
0.32
-
4-nitrophenyl phosphate
-
isozyme B/I, pH 10.0
0.35
-
4-nitrophenyl phosphate
-
pH 8.9, 37C
0.35
-
4-nitrophenyl phosphate
-
isozyme B2, pH 10.0
0.35
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.02 M dimethylamine; pH 9.8, 20C, 0.02 M ethylamine
0.4
-
4-nitrophenyl phosphate
Q7S2X3
37C, pH 9.5, mutant os-1 enzyme, 2 mM MgCl2
0.41
-
4-nitrophenyl phosphate
-
with Mg2+
0.43
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M ethylamine
0.45
-
4-nitrophenyl phosphate
B0R9W3, -
pH 10.5, 20C, 4 M NaCl
0.48
-
4-nitrophenyl phosphate
-
isozyme B1, pH 10.0
0.5
-
4-nitrophenyl phosphate
-
pH 9.2, 45C, Vmax: 0.02 mM/min
0.56
-
4-nitrophenyl phosphate
-
37C, pH 9.8
0.62
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M methylamine
0.65
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M dimethylamine
0.69
-
4-nitrophenyl phosphate
-
pH 10, 37C, Vmax: 0.02 mM/min
0.7
-
4-nitrophenyl phosphate
-
-
0.83
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M diethanolamine
0.85
-
4-nitrophenyl phosphate
-
37C, native enzyme, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.95
-
4-nitrophenyl phosphate
-
pH 9.8, 37C
0.96
-
4-nitrophenyl phosphate
-
pH 10.0, 25C
1.07
-
4-nitrophenyl phosphate
-
pH 10.5, 37C, free-enzyme
1.2
-
4-nitrophenyl phosphate
Q7S2X3
37C, pH 9.5, wild-type enzyme, 2 mM MgCl2
1.37
-
4-nitrophenyl phosphate
-
pH not specified, 37C, Vmax: 0.011 mM/min, in the presence of 0.8 M NaN3
1.43
-
4-nitrophenyl phosphate
-
pH 9.5, 70C, Co2+-combined enzyme
1.51
-
4-nitrophenyl phosphate
-
pH 9.5, 30C, foot
1.58
-
4-nitrophenyl phosphate
-
;
1.91
-
4-nitrophenyl phosphate
-
pH 9.5, 37C, Vmax: 0.029 mM/min, in the presence of 0.8 M KNO3
2.44
-
4-nitrophenyl phosphate
-
pH 10.5, 37C, enzyme immobilized by phosphatase-polyresorcinol complex
2.48
-
4-nitrophenyl phosphate
-
pH 8.5, 30C, digestive gland and siphon
2.48
-
4-nitrophenyl phosphate
-
40% sucrose, -4.5C, frozen
2.5
3
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M N-methylethanolamine
2.52
-
4-nitrophenyl phosphate
-
pH 9.5, 37C, Vmax: 0.023 mM/min, in the presence of 0.8 M KCl
2.54
-
4-nitrophenyl phosphate
-
pH 10, 37C, Vmax: 0.018 mM/min, in the presence of 0.8 M NaAc
2.73
-
4-nitrophenyl phosphate
-
pH 9.25, 37C, Vmax: 0.02 mM/min, in the presence of 0.8 M KPF6
2.8
-
4-nitrophenyl phosphate
-
pH 10, 30C
2.86
-
4-nitrophenyl phosphate
-
pH 9.7, 37C
2.88
-
4-nitrophenyl phosphate
-
pH 8.5, 30C, mantle
2.97
-
4-nitrophenyl phosphate
-
40% sucrose, -4.5C, unfrozen
3.43
-
4-nitrophenyl phosphate
-
pH 9.25, 37C, Vmax: 0.021 mM/min, in the presence of 0.8 M NaNO3
3.6
-
4-nitrophenyl phosphate
-
pH 8, 25C, without phosphate acceptor
4.4
-
4-nitrophenyl phosphate
-
pH 9, 37C, Vmax: 0.016 mM/min, in the presence of 0.8 M NaBF4
4.42
-
4-nitrophenyl phosphate
-
pH 9.5, 37C, Vmax: 0.028 mM/min, in the presence of 0.8 M NaCl
4.52
-
4-nitrophenyl phosphate
-
pH 8.5, 30C, gills
4.59
-
4-nitrophenyl phosphate
-
pH 9.8, recombinant enzyme expressed in Tn-5B1-4 cells
6.4
-
4-nitrophenyl phosphate
-
40% sucrose, 25C
6.76
-
4-nitrophenyl phosphate
-
pH 9.8, recombinant enzyme expressed in Sf-9 cells
6.87
-
4-nitrophenyl phosphate
-
pH 9, 37C, Vmax: 0.022 mM/min, in the presence of 0.8 M Na2SO4
7.32
-
4-nitrophenyl phosphate
-
pH not specified, 37C, Vmax: 0.019 mM/min, in the presence of 0.8 M Na citrate
9
-
4-nitrophenyl phosphate
-
-
49.7
-
4-nitrophenyl phosphate
-
pH 9.8, native placental enzyme
3
-
5'-AMP
-
-
4.5
-
5'-dTMP
-
-
2.26
-
ADP
-
pH 7.4, 37C
0.44
-
Alpha-naphthyl phosphate
-
pH 8.9, 37C
0.1
-
ATP
-
-
0.39
-
ATP
-
membranous enzyme form
0.48
-
ATP
-
soluble enzyme form
2.38
-
ATP
-
pH 7.4, 37C
0.3
-
beta-Glycerophosphate
-
soluble enzyme form
0.38
-
beta-Glycerophosphate
-
membranous enzyme form
1.4
-
beta-Glycerophosphate
-
-
1.5
-
beta-Glycerophosphate
-
purified enzyme
1.9
-
beta-Glycerophosphate
-
pH 7.4, 37C
3
-
beta-Glycerophosphate
-
membrane-bound enzyme
3.35
-
beta-Glycerophosphate
-
-
2.46
-
beta-glyceryl phosphate
-
pH 8.9, 37C
0.12
-
diphosphate
-
purified enzyme
0.21
-
diphosphate
-
membrane-bound enzyme
1.4
-
diphosphate
-
allozyme D, pH 7.5, 37C, in presence of Mg2+ and Zn2+
2.5
-
diphosphate
-
-
4
-
diphosphate
-
-
2.22
-
glucose 1-phosphate
-
-
4.8
-
glucose 1-phosphate
-
-
1.49
-
glucose 6-phosphate
-
-
1.096
-
O-phosphoserine
B4EKR2, -
-
0.806
-
O-Phosphotyrosine
B4EKR2, -
-
0.0094
-
p-nitrophenyl phosphate
-
wild type enzyme, in absence of a phosphate acceptor
0.0154
-
p-nitrophenyl phosphate
-
MOPS buffer
0.02
-
p-nitrophenyl phosphate
-
pH 9.0, hydrophilic and amphiphilic enzyme form
0.021
-
p-nitrophenyl phosphate
-
25C, pH 8.0, wild-type enzyme
0.02124
-
p-nitrophenyl phosphate
-
wild type enzyme, in presence of a phosphate acceptor
0.034
-
p-nitrophenyl phosphate
-
and a second Km value of 0.056 mM
0.037
-
p-nitrophenyl phosphate
Bacillus sp. OK-1
-
-
0.037
-
p-nitrophenyl phosphate
-
pH 9.2, absence of divalent metal ions
0.056
-
p-nitrophenyl phosphate
-
and a second Km value of 0.034 mM
0.05972
-
p-nitrophenyl phosphate
-
mutant enzyme D369N, in presence of a phosphate acceptor
0.08
-
p-nitrophenyl phosphate
-
25C, pH 9.8, wild-type enzyme
0.081
-
p-nitrophenyl phosphate
-
-
0.088
-
p-nitrophenyl phosphate
-
purified enzyme
0.11
-
p-nitrophenyl phosphate
-
isoenzyme III
0.176
-
p-nitrophenyl phosphate
-
mutant enzyme D369N, in absence of a phosphate acceptor
0.183
-
p-nitrophenyl phosphate
-
-
0.19
-
p-nitrophenyl phosphate
-
25C, pH 9.8, mutant enzyme W274K
0.22
-
p-nitrophenyl phosphate
-
isoenzyme II
0.22
-
p-nitrophenyl phosphate
-
pH 10.2, in presence of 1 mM Mn2+
0.252
-
p-nitrophenyl phosphate
-
-
0.28
-
p-nitrophenyl phosphate
-
-
0.33
-
p-nitrophenyl phosphate
B4EKR2, -
-
0.39
-
p-nitrophenyl phosphate
-
membrane-bound enzyme
0.44
-
p-nitrophenyl phosphate
-
membranous enzyme form
0.45
-
p-nitrophenyl phosphate
-
soluble enzyme form
0.62
-
p-nitrophenyl phosphate
-
-
0.8
-
p-nitrophenyl phosphate
-
-
0.8
-
p-nitrophenyl phosphate
-
-
0.8
-
p-nitrophenyl phosphate
-
-
0.94
-
p-nitrophenyl phosphate
-
-
1.114
-
p-nitrophenyl phosphate
-
-
1.25
-
p-nitrophenyl phosphate
-
25C, pH 9.8, mutant enzyme H116D
1.3
-
p-nitrophenyl phosphate
-
-
1.3
-
p-nitrophenyl phosphate
-
-
1.44
-
p-nitrophenyl phosphate
-
25C, pH 9.8, mutant enzyme H116D/W274K
2
-
p-nitrophenyl phosphate
-
isoenzyme I
2.5
-
p-nitrophenyl phosphate
-
-
2.6
-
p-nitrophenyl phosphate
-
-
2.941
-
p-nitrophenyl phosphate
-
mutant enzyme D369A, in absence of a phosphate acceptor
4.48
-
p-nitrophenyl phosphate
-
pH 10.3, hydrophilic enzyme form
5.02
-
p-nitrophenyl phosphate
-
pH 10.3, amphiphilic enzyme form
0.348
-
Paraoxon
-
pH 7.4, 37C
6.1
-
Phenyl phosphate
-
-
6.67
-
Phenyl phosphate
-
enzyme from small intestine
8.7
-
Phenyl phosphate
-
-
9.5
-
Phenyl phosphate
-
-
10.2
-
Phenyl phosphate
-
-
11.63
-
Phenyl phosphate
-
enzyme from 8 day pseudopregant deciduae
11.9
-
Phenyl phosphate
-
enzyme from 20 day term fetal placentae
12.3
-
Phenyl phosphate
-
-
12.4
-
Phenyl phosphate
-
-
13.1
-
Phenyl phosphate
-
enzyme from 8 day pregnant deciduae
16.2
-
Phenyl phosphate
-
-
23.81
-
Phenyl phosphate
-
enzyme from anestrus uterus
0.39
-
phospho-DL-Thr
-
purified enzyme
0.9
-
phospho-DL-Thr
-
membrane-bound enzyme
0.4
-
phospho-DL-Tyr
-
purified enzyme
0.72
-
phospho-DL-Tyr
-
membrane-bound enzyme
0.38
-
phospho-L-Ser
-
purified enzyme
0.68
-
phospho-L-Ser
-
membrane-bound enzyme
0.145
-
phosphoenolpyruvate
B4EKR2, -
-
2.9
-
Phosphoethanolamine
-
-
0.12
-
pyridoxal 5'-phosphate
-
allozyme D, pH 7.5, 37C, in presence of Mg2+ and Zn2+
0.2
-
pyridoxal phosphate
-
purified enzyme
0.37
-
pyridoxal phosphate
-
membrane-bound enzyme
1.47
-
Trehalose 6-phosphate
-
-
0.1159
-
3-(4-methoxyspiro [1,2-dioxetane-3,2'-(5'-chloro)-tricyclo [3.3.1.13,7]-decan]-4-yl)phenyl phosphate
-
glutaraldehyde X-link, immobilized ALP
additional information
-
4-nitrophenyl phosphate
-
the Km values increase with increasing concentrations of diethanolamine and N-methylethanolamine, but not triethanolamine
0.47
-
L-histidinyl phosphate
-
pH 8.9, 37C
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics at several temperatures and pH-value combinations
-
additional information
-
additional information
-
kinetics of other allozymes of PALP
-
additional information
-
additional information
-
kinetic characterization of the homodimeric complementation mutants, and heterodimeric hybrid formation
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
33
-
2'-[2-benzthiazole]-6'-hydroxybenzthiazole phosphate
-
-
0.00021
-
4-nitrophenyl phosphate
-
pH 8.0, 25C, recombinant mutant T59R
0.016
-
4-nitrophenyl phosphate
-
mutant E322K, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.027
-
4-nitrophenyl phosphate
-
mutant E322K, pH 8.0, 25C, in presence of a phosphoryl group acceptor
0.037
0.23
4-nitrophenyl phosphate
-
37C, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
0.042
-
4-nitrophenyl phosphate
-
mutant E341K, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.052
-
4-nitrophenyl phosphate
-
mutant T155M, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.059
-
4-nitrophenyl phosphate
-
mutant H412Y, pH 8.0, 25C, in presence of a phosphoryl group acceptor
0.067
-
4-nitrophenyl phosphate
-
mutant H412Y, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.1
-
4-nitrophenyl phosphate
-
mutant E341K, pH 8.0, 25C, in presence of a phosphoryl group acceptor
0.3
-
4-nitrophenyl phosphate
-
pH 8.0, 25C, mutant R166A
0.32
-
4-nitrophenyl phosphate
-
mutant T155M, pH 8.0, 25C, in presence of a phosphoryl group acceptor
0.39
-
4-nitrophenyl phosphate
-
mutant D369N, pH 8.0, 25C, in absence of a phosphoryl group acceptor
0.5
-
4-nitrophenyl phosphate
-
pH 8.0, 25C, mutant R166S
0.55
-
4-nitrophenyl phosphate
-
10C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
0.65
-
4-nitrophenyl phosphate
-
pH 8.0, 25C, mutant R166K
1.5
-
4-nitrophenyl phosphate
-
pH 8.0, 25C, recombinant mutant T59A
2.3
-
4-nitrophenyl phosphate
-
pH 8.0, 25C, recombinant wild-type enzyme
2.4
-
4-nitrophenyl phosphate
-
mutant D369N, pH 8.0, 25C, in presence of a phosphoryl group acceptor
3.4
-
4-nitrophenyl phosphate
-
25C, pH 8, mutant enzyme T81A
3.8
-
4-nitrophenyl phosphate
-
mutant S105L, pH 8.0, 25C, in absence of a phosphoryl group acceptor
5.8
-
4-nitrophenyl phosphate
-
mutant S105L, pH 8.0, 25C, in presence of a phosphoryl group acceptor
12
-
4-nitrophenyl phosphate
-
pH 8.0, 25C, wild-type
14.67
-
4-nitrophenyl phosphate
-
10C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
16
-
4-nitrophenyl phosphate
-
pH 8.0, 25C
18
-
4-nitrophenyl phosphate
-
25C, pH 10.5, mutant enzyme T81A
20
50
4-nitrophenyl phosphate
-
57C, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
24.39
-
4-nitrophenyl phosphate
-
25C, pH 10.5, mutant enzyme T81A
26
-
4-nitrophenyl phosphate
-
25C, pH10.5, wild-type enzyme
29.9
-
4-nitrophenyl phosphate
-
pH 8, 25C, in the presence of phosphate acceptor (1 M Tris-HCl buffer)
30
-
4-nitrophenyl phosphate
-
pH 10.0, 15C, mutant S86A/G87A
34
-
4-nitrophenyl phosphate
-
25C, pH 8, wild-type enzyme
34
-
4-nitrophenyl phosphate
-
pH 10.5, mutant V406A
36.98
-
4-nitrophenyl phosphate
-
25C, pH 8, mutant enzyme T81A
44.4
-
4-nitrophenyl phosphate
-
wild-type enzyme, pH 8.0, 25C, in absence of a phosphoryl group acceptor
56.3
-
4-nitrophenyl phosphate
-
pH 8.0, 25C, recombinant mutant T59A
61.84
-
4-nitrophenyl phosphate
-
25C, pH 8, wild-type enzyme
65
-
4-nitrophenyl phosphate
-
37C, native enzyme
65.6
-
4-nitrophenyl phosphate
-
mutant D434E, pH 8.0, 25C, in absence of a phosphoryl group acceptor
70
-
4-nitrophenyl phosphate
-
pH 10.0, 15C, mutant S42G/H135E
71
-
4-nitrophenyl phosphate
-
pH 10.0, 15C, mutant S42G/S338T
74.7
-
4-nitrophenyl phosphate
-
pH 8.0, 25C, recombinant wild-type enzyme
76
-
4-nitrophenyl phosphate
-
pH 9.5, 70C, wild-type enzyme
77.4
-
4-nitrophenyl phosphate
-
37C, native enzyme, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
78.83
-
4-nitrophenyl phosphate
-
37C, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
80.5
-
4-nitrophenyl phosphate
-
wild-type enzyme, pH 8.0, 25C, in presence of a phosphoryl group acceptor
87.83
-
4-nitrophenyl phosphate
-
57C, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
100
-
4-nitrophenyl phosphate
-
pH 8.0, 65C
100
-
4-nitrophenyl phosphate
-
pH 10.0, 15C, mutant G87A
113.6
-
4-nitrophenyl phosphate
P00634
single-chain Fv antibody fusion protein
114
-
4-nitrophenyl phosphate
-
pH 10.0, 15C, mutant S338T
115.9
-
4-nitrophenyl phosphate
-
37C, native enzyme
117
-
4-nitrophenyl phosphate
-
pH 10.0, 15C, mutant G149D
132
-
4-nitrophenyl phosphate
-
25C, pH 8.0, mutant enzyme G51C
133
-
4-nitrophenyl phosphate
-
pH 10.0, 15C, mutant S42G
140
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.05 M methylamine
150
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.02 M dimethylamine
153.9
-
4-nitrophenyl phosphate
-
37C, enzyme with aliphatic-group modification by 3,3',4,4'-tetracarboxylic acid in a photo-assisted reaction
155.7
-
4-nitrophenyl phosphate
-
10C, native enzyme
183.3
-
4-nitrophenyl phosphate
-
57C, native enzyme
190
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.05 M diethanolamine
203
-
4-nitrophenyl phosphate
-
pH 10.0, 15C, mutant S86A
204
-
4-nitrophenyl phosphate
-
25C, pH 8.0, mutant enzyme S52C
217
-
4-nitrophenyl phosphate
-
25C, pH 8.0, mutant enzyme S53C
236
-
4-nitrophenyl phosphate
-
pH 10.0, 15C, wild-type
300
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M ethanolamine
303
-
4-nitrophenyl phosphate
-
pH 10.0, 15C, mutant H135E
330
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M methylamine
350
-
4-nitrophenyl phosphate
-
pH 10.0, 25C
350
-
4-nitrophenyl phosphate
-
25C, pH 8.0, mutant enzyme I50C
361
-
4-nitrophenyl phosphate
-
pH 10.0, 15C, mutant H135E/G149D
370
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M dimethylamine
379
-
4-nitrophenyl phosphate
-
allozyme D, pH 9.8, in presence of Mg2+ and Zn2+
400
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M ethylamine
450
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.02 M ethylamine
500
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.2 M N-methylethanolamine
610
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.05 M ethanolamine
812.3
-
4-nitrophenyl phosphate
-
37C, native enzyme
840
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 0.1 M triethanolamine
971
-
4-nitrophenyl phosphate
-
pH 10.5, wild-type
1130
-
4-nitrophenyl phosphate
-
pH 9.5, 70C, Co2+-combined enzyme
1240
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M diethanolamine
1443
-
4-nitrophenyl phosphate
-
37C, enzyme with amino-group modification in the dark, pH 7, with 12.5 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
1450
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M triethanolamine
2086
-
4-nitrophenyl phosphate
-
25C, pH 8.0, wild-type enzyme
2250
-
4-nitrophenyl phosphate
-
pH 9.8, 20C, 1 M N-methylethanolamine
16230
-
4-nitrophenyl phosphate
-
37C, native enzyme, enzyme with amino-group modification in the dark, pH 8, with 6.25 mM 3,3',4,4'-benzophenone tetracarboxylic dianhydride
48.3
-
O-phosphoserine
B4EKR2, -
-
138.1
-
O-Phosphotyrosine
B4EKR2, -
-
0.01
-
p-nitrophenyl phosphate
-
mutant enzyme D369A, in absence of a phosphate acceptor
0.4
-
p-nitrophenyl phosphate
-
mutant enzyme D369N, in absence of a phosphate acceptor
38
-
p-nitrophenyl phosphate
-
25C, pH 8.0, wild-type enzyme
44.5
-
p-nitrophenyl phosphate
-
wild type enzyme
80.5
-
p-nitrophenyl phosphate
-
wild type enzyme, in presence of a phosphate acceptor
147.9
-
p-nitrophenyl phosphate
B4EKR2, -
-
220
-
p-nitrophenyl phosphate
-
25C, pH 9.8, mutant enzyme W274K
230
-
p-nitrophenyl phosphate
-
mutant enzyme D369N, in presence of a phosphate acceptor
830
-
p-nitrophenyl phosphate
-
25C, pH 9.8, mutant enzyme H116D
930
-
p-nitrophenyl phosphate
-
25C, pH 9.8, mutant enzyme H116D/W274K
1580
-
p-nitrophenyl phosphate
-
25C, pH 9.8, wild-type enzyme
14.1
-
phosphoenolpyruvate
B4EKR2, -
-
92
-
pyridoxal 5'-phosphate
-
allozyme D, pH 7.5, 37C, in presence of Mg2+ and Zn2+
244
-
diphosphate
-
allozyme D, pH 7.5, 37C, in presence of Mg2+ and Zn2+
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kcat/KM (1/Msec) wild-type: 140000, mutant R166K: 20, mutant R166S: 24
-
additional information
-
additional information
-
wild-type enzyme: kcat/KM (1/M*sec) (4-nitrophenyl phosphate): 33000000, (3-nitrobenzyl phosphate): 18000000, (methyl phosphate): 1200000, (methyl 4-nitrophenyl phosphate): 18, (bis-4-nitrophenyl phosphate): 0.05, (4-nitrophenyl sulfate): 0.01
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3810
-
4-nitrophenyl phosphate
P00634
single-chain Fv antibody fusion protein
4742
40.8
-
O-phosphoserine
B4EKR2, -
-
14721
171
-
O-Phosphotyrosine
B4EKR2, -
-
14722
448
-
p-nitrophenyl phosphate
B4EKR2, -
-
15065
94.4
-
phosphoenolpyruvate
B4EKR2, -
-
15572
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.135
-
6-(1-benzothiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole
-
-
0.085
-
6-(1-benzothiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole
-
-
0.000261
-
arsenate
-
pH 9.5, 37C, standard spectrophotometric assays
0.0089
-
arsenate
-
pH 9.5, 37C, ALP immobilized capillary electrophoresis, Ki value is close to the Ki values obtained by the standard spectrophotometric assay
7e-05
-
bis(1,1,1-trifluoroacetylacetonato)oxovanadium(IV)
-
pH 8, 37C
0.00015
-
bis(3-chloroacetylacetonato)oxovanadium(IV)
-
pH 8, 37C
0.00104
-
bis(3-chloroacetylacetonato)oxovanadium(IV)(4-Mepy)
-
pH 8, 37C
0.00034
-
bis(3-methylacetylacetonato)oxovanadium(IV)
-
pH 8, 37C
0.00043
-
bis(acetylacetonato)oxovanadium(IV)
-
pH 8, 37C
0.00069
-
bis(acetylacetonato)oxovanadium(IV)(4-Mepy)
-
pH 8, 37C
0.0004
-
bis(benzoylacetonato)oxovanadium(IV)
-
pH 8, 37C
17.4
-
Caffeine
-
pH 9.8, 25C
3.16e-07
-
Cry1Ac toxin
-
competitive inhibition; competitive inhibition
-
3.33
-
HPO42-
-
37C, pH 9.8
5
-
imidazole
-
pH 9.8, 25C
0.0011
-
Inorganic phosphate
-
pH 8.0, 25C, wild-type
-
0.075
-
Inorganic phosphate
-
pH 8.0, 25C, mutant R166K
-
0.46
-
Inorganic phosphate
-
pH 8.0, 25C, mutant R166S
-
0.65
-
Inorganic phosphate
-
pH 8.0, 25C, mutant R166A
-
5.4
-
L-leucine
-
pH 9.8, 25C
3.18
-
L-Phe
-
37C, pH 9.8
3
-
L-phenylalanine
-
pH 9.8, 25C
1.74
-
lansoprazole
-
-
0.093
-
levamisole
-
-
4
-
MnO4-
-
pH 9.8, 25C
0.00049
-
Na3VO4
-
pH 8, 37C
0.9
-
NaH2PO4
-
pH 9.2, 45C
0.012
-
Na[VO(O2)2(asparagine)]H2O
-
pH 10, 30C
0.013
-
Na[VO(O2)2(glutamine)]H2O
-
pH 10, 30C
0.01
-
Na[VO(O2)2(glycyl-glycine)(H2O)]H2O
-
pH 10, 30C
0.006
-
Na[VO(O2)2(triglycine)]3H2O
-
pH 10, 30C
0.0425
-
orthovanadate
-
-
0.00241
-
phosphate
-
pH 9.5, 37C, ALP immobilized capillary electrophoresis, Ki value is close to the Ki values obtained by the standard spectrophotometric assay
0.00311
-
phosphate
-
pH 9.5, 37C, standard spectrophotometric assays
0.0053
-
phosphate
-
IAPase
0.0061
-
phosphate
-
25C, pH 8, wild-type enzyme
0.0065
-
phosphate
-
25C, pH 8, mutant enzyme T81A
0.027
-
phosphate
-
25C, pH 8.0, mutant enzyme G51C
0.03
-
phosphate
-
25C, pH 8.0, mutant enzyme I50C
0.034
-
phosphate
-
25C, pH 8.0, mutant enzyme S52C
0.045
-
phosphate
-
25C, pH 8.0, wild-type enzyme
0.0472
-
phosphate
-
pH 8.0, 25C
0.069
-
phosphate
-
pH 10.5, 37C, free-enzyme
0.1
-
phosphate
-
25C, pH 8.0, mutant enzyme S53C; 25C, pH 8.0, wild-type enzyme
0.1
-
phosphate
-
25C, pH 10.5, wild-type enzyme
0.14
-
phosphate
-
25C, pH 10.5, mutant enzyme T81A
0.39
-
phosphate
-
25C, pH 9.8, wild-type enzyme
0.423
-
phosphate
-
pH 10.5, 37C, enzyme immobilized by phosphatase-polyresorcinol complex
0.55
-
phosphate
Q7S2X3
37C, pH 9.5, mutant os-1 enzyme
0.56
-
phosphate
B0R9W3, -
pH 10.5, 20C, 4 M NaCl
0.76
-
phosphate
-
CAPase
0.77
-
phosphate
-
25C, pH 9.8, mutant enzyme W274K
1.6
-
phosphate
Q7S2X3
37C, pH 9.5, wild-type enzyme
1.7
-
phosphate
-
pH 8.0, 25C
2
-
phosphate
-
pH 9.8, 25C
3.45
-
phosphate
-
25C, pH 9.8, mutant enzyme H116D/W274K
5.25
-
phosphate
-
25C, pH 9.8, mutant enzyme H116D
0.05
-
theophylline
-
pH 9.5, 37C, ALP immobilized capillary electrophoresis, Ki value is close to the Ki values obtained by the standard spectrophotometric assay
0.096
-
theophylline
-
pH 9.5, 37C, standard spectrophotometric assays
0.00056
-
vanadate
Q7S2X3
37C, pH 9.5, wild-type enzyme
0.0075
-
vanadate
Q7S2X3
37C, pH 9.5, mutant os-1 enzyme
0.00055
-
VOSO4
-
pH 8, 37C
0.0147
-
[WO(O2)2(glycyl-glycine)(H2O)]3H2O
-
pH 10, 30C
0.0118
-
[WO(O2)2(triglycine)]3H2O
-
pH 10, 30C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.00149
-
1,4-dimethoxy-2-methylbenzene
-
-
-
0.0012
-
1-(3,4-dihydroxyphenyl)-2-(1H-imidazol-1-yl)ethanone
-
-
-
0.0021
-
1-(3,4-dihydroxyphenyl)-2-(1H-imidazol-1-yl)ethanone
-
-
-
0.0302
-
1-(3,4-dihydroxyphenyl)-2-(1H-imidazol-1-yl)ethanone
-
-
-
0.0042
-
1-(3,4-dihydroxyphenyl)-2-(2-ethyl-1H-imidazol-1-yl)ethanone
-
-
-
0.0012
-
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-benzimidazol-1-yl)ethanone
-
-
0.0263
-
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-benzimidazol-1-yl)ethanone
-
-
0.0033
-
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-imidazol-1-yl)ethanone
-
-
0.0646
-
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-imidazol-1-yl)ethanone
-
-
0.0783
-
1-(3,4-dihydroxyphenyl)-2-(2-methyl-1H-imidazol-1-yl)ethanone
-
-
0.0172
-
1-(3,4-dihydroxyphenyl)-2-(2-phenyl-1H-imidazol-1-yl)ethanone
-
-
-
0.0058
-
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-imidazol-1-yl)ethanone
-
-
-
0.0411
-
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-imidazol-1-yl)ethanone
-
-
-
0.0027
-
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-pyrazol-1-yl)ethanone
-
-
-
0.0533
-
1-(3,4-dihydroxyphenyl)-2-(4-methyl-1H-pyrazol-1-yl)ethanone
-
-
-
0.0134
-
1-(3,4-dihydroxyphenyl)-2-(4H-1,2,4-triazol-4-yl)ethanone
-
-
-
0.0058
-
1-(3,4-dihydroxyphenyl)-2-(5,6-dimethyl-1H-benzimidazol-1-yl)ethanone
-
-
0.0393
-
1-(3,4-dihydroxyphenyl)-2-(propan-2-ylamino)ethanone
-
-
0.0006
-
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
-
-
-
0.0025
-
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
-
-
-
0.0086
-
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
-
-
-
0.0495
-
1-(3,4-dihydroxyphenyl)-2-[(4,6-dimethylpyrimidin-2-yl)sulfanyl]ethanone
-
-
-
0.0067
-
1-(3,4-dihydroxyphenyl)-2-[(4-methyl-5-phenyl-4H-1,2,4-triazol-3-yl)sulfanyl]ethanone
-
-
-
0.002
-
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
-
-
-
0.008
-
1-(3,4-dihydroxyphenyl)-2-[[1-(4-methoxyphenyl)-1H-tetrazol-5-yl]sulfanyl]ethanone
-
-
-
0.00069
-
1-chloro-4-ethoxy-2-methylbenzene
-
-
0.00051
-
1-chloro-4-methoxy-2-methylbenzene
-
-
-
0.00129
-
1-fluoro-4-methoxybenzene
-
-
0.000488
-
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-ethylpiperazine
P09487
-
0.000828
-
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]-4-methylpiperazine
P09487
-
0.00145
-
1-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]azepane
P09487
-
0.00019
-
2,5-dimethoxy-N-(quinolin-3-yl)benzenesulfonamide
-
-
-
0.00106
-
2,5dimethoxy-N-(pyridin-3-yl)benzenesulfonamide
-
-
-
0.0008
-
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
0.0027
-
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
0.0148
-
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
0.018
-
2-(1H-benzimidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
0.0062
-
2-(1H-benzimidazol-2-ylamino)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
0.0091
-
2-(1H-benzimidazol-2-ylamino)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
0.0938
-
2-(1H-benzimidazol-2-ylamino)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
0.0158
-
2-(4-bromo-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
0.0475
-
2-(4-bromo-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
0.0049
-
2-(4-bromo-2-methyl-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
0.0087
-
2-(4-bromo-2-methyl-1H-imidazol-1-yl)-1-(3,4-dihydroxyphenyl)ethanone
-
-
-
0.000375
-
2-(4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]piperazin-1-yl)ethanol
P09487
-
0.00113
-
2-chloro-1,4-dimethoxybenzene
-
-
0.00113
-
2-ethoxy-5-methyl-N-(pyridin-3-yl)benzenesulfonamide
-
-
-
18
-
2-glycerophosphate
-
-
0.00316
-
2-methoxy-4-nitro-N-(pyridin-3-yl)benzenesulfonamide
-
-
-
0.00074
-
2-methoxy-4-nitro-N-(quinolin-3-yl)benzenesulfonamide
-
-
-
0.00185
-
2-methoxy-5-methyl-N-(pyridin-3-yl)benzenesulfonamide
-
-
-
0.00065
-
2-methoxy-5-methyl-N-(quinolin-3-yl)benzenesulfonamide
-
-
-
0.0022
-
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
-
-
-
0.0048
-
2-[[2-(3,4-dihydroxyphenyl)-2-oxoethyl]sulfanyl]-4-(methoxymethyl)-6-methylpyridine-3-carbonitrile
-
-
-
0.000127
-
3-(2,4-dichloro-5-fluorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
P09487
-
0.000324
-
3-(2,4-dichloro-5-fluorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
P09487
-
0.00485
-
3-(2,4-dichloro-5-fluorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
P09487
-
0.0001
-
3-(2,4-dichloro-5-fluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
P09487
-
5.6e-05
-
3-(2,4-dichloro-5-fluorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
P09487
-
4.4e-05
-
3-(2,4-dichlorophenyl)-1H-pyrazole-5-carbohydrazide
P09487
-
4.7e-05
-
3-(2,4-dichlorophenyl)-N,N-bis(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
P09487
-
0.000285
-
3-(2,4-dichlorophenyl)-N,N-diethyl-1H-pyrazole-5-carboxamide
P09487
-
0.000119
-
3-(2,4-dichlorophenyl)-N,N-dimethyl-1H-pyrazole-5-carboxamide
P09487
-
5.1e-05
-
3-(2,4-dichlorophenyl)-N-(1-methylethyl)-1H-pyrazole-5-carboxamide
P09487
-
4.4e-05
-
3-(2,4-dichlorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
P09487
-
4.6e-05
-
3-(2,4-dichlorophenyl)-N-(2-methoxyethyl)-1H-pyrazole-5-carboxamide
P09487
-
8.2e-05
-
3-(2,4-dichlorophenyl)-N-(2-methylpropyl)-1H-pyrazole-5-carboxamide
P09487
-
3.1e-05
-
3-(2,4-dichlorophenyl)-N-(3-hydroxypropyl)-1H-pyrazole-5-carboxamide
P09487
-
0.000459
-
3-(2,4-dichlorophenyl)-N-(3-methylbutyl)-1H-pyrazole-5-carboxamide
P09487
-
3.5e-05
-
3-(2,4-dichlorophenyl)-N-(4-hydroxybutyl)-1H-pyrazole-5-carboxamide
P09487
-
3.5e-05
-
3-(2,4-difluorophenyl)-N-(2-hydroxyethyl)-1H-pyrazole-5-carboxamide
P09487
-
0.8
-
3-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
pH 10.4, 37C, value higher than 0.8 mM; pH 7.8, 37C, value higher than 0.8 mM
0.003
-
3-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
-
-
-
0.0292
-
3-[2-(3,4-dihydroxyphenyl)-2-oxoethyl]-6,7-dimethoxy-2-benzofuran-1(3H)-one
-
-
-
0.00155
-
4-bromo-2,5-dimethoxy-N-(pyridin-3-yl)benzenesulfonamide
-
-
0.00168
-
4-methoxy-1,2-dimethylbenzene
-
-
0.0512
-
4-[[(4,6-dimethylpyrimidin-2-yl)amino]methyl]benzene-1,2-diol
-
-
0.000574
-
4-[[3-(2,4-dichlorophenyl)-1H-pyrazol-5-yl]carbonyl]morpholine
P09487
-
0.00012
-
5-bromo-2-methoxy-N-(quinolin-3-yl)benzenesulfonamide
-
-
0.00054
-
5-chloro-2-ethoxy-N-(pyridin-3-yl)benzenesulfonamide
-
-
-
0.8
-
6-(thiophen-2-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
pH 10.4, 37C, value higher than 0.8 mM; pH 7.8, 37C, value higher than 0.8 mM
0.26
-
6-(thiophen-2-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
pH 7.8, 37C
0.331
-
6-(thiophen-2-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
pH 10.4, 37C
0.192
-
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
pH 7.8, 37C
0.408
-
6-(thiophen-3-yl)-2,3,5,6-tetrahydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
pH 10.4, 37C
0.8
-
6-(thiophen-3-yl)-2,3-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
pH 10.4, 37C, value higher than 0.8 mM; pH 7.8, 37C, value higher than 0.8 mM
0.042
-
6-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
pH 10.4, 37C
0.084
-
6-(thiophen-3-yl)-5,6-dihydroimidazo[2,1-b][1,3]thiazole hydrochloride
-
pH 7.8, 37C
0.8
-
6-(thiophen-3-yl)imidazo[2,1-b][1,3]thiazole hydrochloride
-
pH 10.4, 37C, value higher than 0.8 mM; pH 7.8, 37C, value higher than 0.8 mM
2.26
-
EDTA
-
IC50: 2.26 mM
0.078
-
levamisole
-
pH 7.8, 37C
5e-06
-
N-(2-hydroxyethyl)-3-(2,3,4-trichlorophenyl)-1H-pyrazole-5-carboxamide
P09487
-
0.000134
-
N-(2-hydroxyethyl)-3-(2,4,5-trifluorophenyl)-1H-pyrazole-5-carboxamide
P09487
-
0.000398
-
N-tert-butyl-3-(2,4-dichlorophenyl)-1H-pyrazole-5-carboxamide
P09487
-
0.0129
-
Na2[W2O3(O2)4(glycyl-glycine)2](3H2O)
-
pH 10, 30C
0.01267
-
Na2[W2O3(O2)4(glycyl-leucine)2](3H2O)
-
pH 10, 30C
0.015
-
Na[VO(O2)2(asparagine)]H2O
-
pH 10, 30C
0.0165
-
Na[VO(O2)2(glutamine)]H2O
-
pH 10, 30C
0.0118
-
Na[VO(O2)2(glycyl-glycine)(H2O)]H2O
-
pH 10, 30C
0.0025
-
Na[VO(O2)2(triglycine)]3H2O
-
pH 10, 30C
2.8
-
phosphate
-
pH 10.5, 37C, free-enzyme
4
-
phosphate
-
pH 10.5, 37C, enzyme immobilized by phosphatase-polyresorcinol complex
0.03168
-
tungstate
-
pH 10, 30C
0.02534
-
tungstate/H2O2
-
pH 10, 30C
-
0.01584
-
[WO(O2)2(glycyl-glycine)(3H2O)]
-
pH 10, 30C
-
0.0142
-
[WO(O2)2(glycyl-glycine)(H2O)]3H2O
-
pH 10, 30C
0.0198
-
[WO(O2)2(glycyl-leucine)(3H2O)]
-
pH 10, 30C
-
0.0049
-
[WO(O2)2(triglycine)]3H2O
-
pH 10, 30C