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Information on EC 6.2.1.8 - oxalate-CoA ligase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38137

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EC Tree
     6 Ligases
         6.2 Forming carbon-sulfur bonds
             6.2.1 Acid-thiol ligases
                6.2.1.8 oxalate-CoA ligase
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P38137 not found.
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Word Map
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
oxalyl-coa synthetase, acyl-activating enzyme 3, acyl activating enzyme3, scaae3, acyl-activating enzyme3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acyl-activating enzyme 3
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Oxalyl-CoA synthetase
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OCS
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-
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Oxalate:CoA ligase (AMP)
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-
-
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Oxalyl CoA synthetase
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-
-
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Oxalyl coenzyme A synthetase
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-
-
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Oxalyl-CoA synthetase
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-
-
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Synthetase, oxalyl coenzyme A
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
oxalate:CoA ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
37318-57-3
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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
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
show the reaction diagram
-
-
-
?
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
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.02
oxalate
pH 7.5, temperature not specified in the publication
additional information
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
activity range, profile overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene YBR222C
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
a Scaae3 deletion mutant strain shows highly reduced oxalate degradation activity decreasing recovery from exposure to oxalate, e.g. by exposure to oxalate-secreting microbes, and to oxidative stress, e.g. by H2O2
physiological function
the enzyme catalyzes the first step in a pathway of oxalate degradation to protect the cell against the harmful effects of oxalate derived from an endogenous process or an environmental source
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BLR(DE3) by nickel affinity chromatography to over 90% purity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene YBR222C, expression of His-tagged enzyme in Escherichia coli strain BLR(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
oxalate induced the enzyme, quantitative RT-PCR reveals that ScAAE3 transcript levels are induced within min of exposure peaking at about 1 h before declining back to steady state levels
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Foster, J.; Nakata, P.A.
An oxalyl-CoA synthetase is important for oxalate metabolism in Saccharomyces cerevisiae
FEBS Lett.
588
160-166
2014
Saccharomyces cerevisiae (P38137), Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741 (P38137)
Manually annotated by BRENDA team