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Information on EC 3.6.1.7 - acylphosphatase and Organism(s) Escherichia coli and UniProt Accession P0AB65

for references in articles please use BRENDA:EC3.6.1.7
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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.7 acylphosphatase
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This record set is specific for:
Escherichia coli
UNIPROT: P0AB65 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
acylphosphatase, acyp2, sso acp, acyl phosphatase, phacp, acetylphosphatase, acpdro2, acetyl phosphatase, human common-type acylphosphatase, isozyme ch1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,3-diphosphoglycerate phosphatase
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acetic phosphatase
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acetyl phosphatase
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acetylphosphatase
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ACP
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acyl phosphatase
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acyl phosphate phosphohydrolase
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Acylphosphatase, erythrocyte isozyme
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Acylphosphatase, erythrocyte/testis isozyme
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Acylphosphate phosphohydrolase
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acylphosphate phosphomonohydrolase
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carbamoylphosphate phosphatase
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carbamyl phosphate phosphatase
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Isozyme CH1
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Isozyme CH2
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Isozyme TU1
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phosphatase, acyl
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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SYSTEMATIC NAME
IUBMB Comments
acylphosphate phosphohydrolase
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CAS REGISTRY NUMBER
COMMENTARY hide
9012-34-4
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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
acylphosphate + H2O
carboxylate + phosphate
show the reaction diagram
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specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Uniprot
Manually annotated by BRENDA team
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C5A/C49A
site-directed mutagenesis, the folding of the mutant lacking the disulfide bond is impaired and conformational stability is decreased compared to the wild-type enzyme, mutEcoAcP folds about 1500fold slower and a partially folded species accumulates int he mutant expressing strain
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
folding and unfolding kinetics of wild-type and mutant enzymes at 28°C and pH 5.5 as a function of GdnHCl concentration, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stefani, M.; Ramponi, G.
Acylphosphate phosphohydrolases
Life Chem. Rep.
12
271-301
1995
Anas platyrhynchos, Bos taurus, Cavia porcellus, Chondrichthyes, Equus caballus, Escherichia coli, Gallus gallus, Homo sapiens, Meleagris gallopavo, Oryctolagus cuniculus, Rattus norvegicus, Saccharomyces cerevisiae, Sus scrofa, Vigna unguiculata
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Manually annotated by BRENDA team
Parrini, C.; Bemporad, F.; Baroncelli, A.; Gianni, S.; Travaglini-Allocatelli, C.; Kohn, J.E.; Ramazzotti, M.; Chiti, F.; Taddei, N.
The folding process of acylphosphatase from Escherichia coli is remarkably accelerated by the presence of a disulfide bond
J. Mol. Biol.
379
1107-1118
2008
Escherichia coli (P0AB65), Escherichia coli
Manually annotated by BRENDA team