Information on EC 1.2.1.B29 - formate dehydrogenase (NADP+, ferredoxin)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Clostridium autoethanogenum

EC NUMBER
COMMENTARY hide
1.2.1.B29
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
formate dehydrogenase (NADP+, ferredoxin)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster = 2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
formate:NADP+, ferredoxin oxidoreductase
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
S5Z061: [FeFe]-hydrogenase subunit HytA, S5YUC5: formate dehydrogenase subunit FdhA
S5Z061 and S5YUC5
UniProt
Manually annotated by BRENDA team
S5Z061: [FeFe]-hydrogenase subunit HytA, S5YUC5: formate dehydrogenase subunit FdhA
S5Z061 and S5YUC5
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
2 formate + NAD+ + 2 oxidized ferredoxin [iron-sulfur] cluster
2 CO2 + NADH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
show the reaction diagram
2 formate + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
2 CO2 + NADPH + H+ + 2 reduced ferredoxin [iron-sulfur] cluster
show the reaction diagram
H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster
show the reaction diagram
H2 + NADP+ + 2 oxidized methyl viologen
? + NADPH + H+ + 2 reduced methyl viologen
show the reaction diagram
NADPH + 3 H+ + 2 reduced ferredoxin [iron-sulfur] cluster
H2 + NADP+ + 2 oxidized ferredoxin [iron-sulfur] cluster
show the reaction diagram
S5Z061 and S5YUC5
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
S5Z061 and S5YUC5
Km value is above 1 mM, NADPH is preferred over NADH
NADPH
S5Z061 and S5YUC5
Km value is below 0.5 mM, NADPH is preferred over NADH
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
S5Z061 and S5YUC5
formate formation reaction, pH 7.5, 37°C
8.7
S5Z061 and S5YUC5
H2 formation reaction, pH 7.5, 37°C
13
S5Z061 and S5YUC5
substrate H2, pH 6.5, 37°C
15.2
S5Z061 and S5YUC5
substrate formate, pH 7.5, 37°C
26.5
S5Z061 and S5YUC5
H2 formation reaction, pH 6.0, 37°C
29.2
S5Z061 and S5YUC5
substrate H2, pH 7.5, 37°C
32
S5Z061 and S5YUC5
substrate H2, pH 6.5, 37°C
35
S5Z061 and S5YUC5
formate formation, substrates CO2 and H2, pH 7.5, 37°C
41
S5Z061 and S5YUC5
formate formation, substrates CO2 and H2, pH 7.0, 37°C
18000
S5Z061 and S5YUC5
substrates H2 and methyl viologen, pH 7.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
S5Z061 and S5YUC5
H2 formation from formate; H2 formation from NADPH and reduced ferredoxin
6.5
S5Z061 and S5YUC5
NADP and ferredoxin reduction with H2
7
S5Z061 and S5YUC5
CO2 reduction with H2 to formate
7.5
S5Z061 and S5YUC5
NADP and ferredoxin reduction with formate at pH 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
S5Z061 and S5YUC5
assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is rapidly inactivated in the presence of only trace amounts of O2, and it loses activity upon dilution to much below 1 mg/ml even under strictly anoxic conditions
S5Z061 and S5YUC5
734087
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
-
S5Z061 and S5YUC5