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Information on EC 3.6.1.1 - inorganic diphosphatase

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.1 inorganic diphosphatase
IUBMB Comments
Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). cf. EC 7.1.3.1, H+-exporting diphosphatase.
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This record set is specific for:
UNIPROT: Q8A5V9
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
pyrophosphatase, inorganic pyrophosphatase, v-ppase, h+-ppase, vacuolar h(+)-pyrophosphatase, sppase, e-ppase, vacuolar h(+)-ppase, soluble inorganic pyrophosphatase, ippase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
inorganic pyrophosphatase
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H+-PPase
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inorganic diphosphatase
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inorganic pyrophosphatase
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PPase
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pyrophosphatase, inorganic
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Pyrophosphate phospho-hydrolase
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-
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Pyrophosphate phosphohydrolase
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Pyrophosphate-energized inorganic pyrophosphatase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
diphosphate phosphohydrolase
Specificity varies with the source and with the activating metal ion. The enzyme from some sources may be identical with EC 3.1.3.1 (alkaline phosphatase) or EC 3.1.3.9 (glucose-6-phosphatase). cf. EC 7.1.3.1, H+-exporting diphosphatase.
CAS REGISTRY NUMBER
COMMENTARY hide
9024-82-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
diphosphate + H2O
2 phosphate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
diphosphate + H2O
2 phosphate
show the reaction diagram
in vivo function as an inorganic diphosphatase. Substrate discrimination is based, in part, on active site space restrictions imposed by the cap domain, specifically by residues Tyr76 and Glu47
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
required, functions in catalysis and binding structure, overview
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.32
diphosphate
pH 7.5, 25°C, recombinant wild-type BT2127
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.6
diphosphate
pH 7.5, 25°C, recombinant wild-type BT2127
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
89
diphosphate
pH 7.5, 25°C, recombinant wild-type BT2127
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
enzyme BT2127 is a member of the haloalkanoate dehalogenase superfamily, HADSF
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q8A5V9_BACTN
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)
224
0
24939
TrEMBL
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged wild-type and mutant BT2127 variants, sitting-drop vapor diffusion method, X-ray diffraction structure determination and analysis at
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D11N
site-directed mutagenesis, inactive mutant
D13A
site-directed mutagenesis, inactive mutant
D13N
site-directed mutagenesis, inactive mutant
E47A
site-directed mutagenesis, inactive mutant
E47D
site-directed mutagenesis, inactive mutant
E47N
site-directed mutagenesis, inactive mutant
E47Q
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
H23A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
K147A
site-directed mutagenesis, inactive mutant
K79A
site-directed mutagenesis, inactive mutant
M20A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
M20K
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
M20L
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
N172A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
Q117A
site-directed mutagenesis, inactive mutant
R49A
site-directed mutagenesis, inactive mutant
S115A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
S19A
site-directed mutagenesis, inactive mutant
S80A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
T113A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
T50A
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
Y76F
site-directed mutagenesis, inactive mutant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by anion exchange chromatography, hydrophobic interaction chromatography, and nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
phylogenetic analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Huang, H.; Patskovsky, Y.; Toro, R.; Farelli, J.D.; Pandya, C.; Almo, S.C.; Allen, K.N.; Dunaway-Mariano, D.
Divergence of structure and function in the haloacid dehalogenase enzyme superfamily: Bacteroides thetaiotaomicron BT2127 is an inorganic pyrophosphatase
Biochemistry
50
8937-8949
2011
Bacteroides thetaiotaomicron (Q8A5V9), Bacteroides thetaiotaomicron, Bacteroides thetaiotaomicron ATCC 29148 (Q8A5V9)
Manually annotated by BRENDA team