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Information on EC 3.1.3.1 - alkaline phosphatase and Organism(s) Bacillus subtilis and UniProt Accession P19406

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.1 alkaline phosphatase
IUBMB Comments
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)
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Bacillus subtilis
UNIPROT: P19406
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
ap, alkaline phosphatase, bone alkaline phosphatase, placental alkaline phosphatase, alpase, apase, intestinal alkaline phosphatase, tnsalp, phosphomonoesterase, secreted alkaline phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkaline phosphatase 4
-
alkaline phosphatase IV
-
alkaline phenyl phosphatase
-
-
-
-
alkaline phosphohydrolase
-
-
-
-
alkaline phosphomonoesterase
-
-
-
-
ALP
-
-
-
-
AP-TNAP
-
-
-
-
APase
-
-
-
-
APASED
-
-
-
-
BC6
-
-
-
-
EAP
-
-
-
-
Germ-cell alkaline phosphatase
-
-
-
-
glycerophosphatase
-
-
-
-
H-AP
-
-
-
-
High molecular weight phosphatase
-
-
-
-
IAP
-
-
-
-
L-AP
-
-
-
-
Liver/bone/kidney isozyme
-
-
-
-
Low molecular weight phosphatase
-
-
-
-
M-ALP
-
-
-
-
Nagao isozyme
-
-
-
-
non-specific alkaline phosphatase
-
-
-
-
phosphatase, alkaline
-
-
-
-
phosphomonoesterase
-
-
-
-
PLAP-like
-
-
-
-
RAN1
-
-
-
-
Regan isozyme
-
-
-
-
TNSALP
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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)
CAS REGISTRY NUMBER
COMMENTARY hide
9001-78-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
required. In the absence of Co2+ in the lysis buffer, activity of extracts is only 10% of the normal value
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
515
pH 11, 25°C, presence of 0.8-2 M NaCl
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, stable for at least one month
4°C, cell-free extract, stable for two weeks
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
buffers need to be supplemented with 0.1 mM CoCl2. If Co2+ is omitted in the lysis buffer, activity of the cell-free extracts is only about 10% of the normal value. Addition of the absent metal to these extracts restores 100% activity, after overnight incubation at 4°C
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
overexpression of enzyme in Escherichia coli. After 1 day of growth, when the Escherichia coli culture is near the stationary phase, high amounts of enzyme are produced but the alkaline phosphatase activity in the cell-free extract is near the background level. Further incubation of bacterial culture leads to a tremendous increase in alkaline phosphatase activity which is maximal at the 3rd day of incubation and was 48–100 times higher than at the 1st day of growth. Typically, 90-140 mg of active protein is produced in 1 l of culture
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Coleman, J.E.; Gettins, P.
Alkaline phosphatase, solution structure, and mechanism
Adv. Enzymol. Relat. Areas Mol. Biol.
55
381-452
1983
Bacillus subtilis, Bacillus licheniformis, Bos taurus, Escherichia coli, Homo sapiens, Micrococcus sodonensis, Rattus norvegicus
Manually annotated by BRENDA team
Koksharov, M.; Lv, C.; Zhai, X.; Ugarova, N.; Huang, E.
Bacillus subtilis alkaline phosphatase IV acquires activity only late at the stationary phase when produced in Escherichia coli. Overexpression and characterization of the recombinant enzyme
Protein Expr. Purif.
90
186-194
2013
Bacillus subtilis (P19406), Bacillus subtilis, Bacillus subtilis 168 (P19406)
Manually annotated by BRENDA team