Information on EC 1.2.7.5 - aldehyde ferredoxin oxidoreductase

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The expected taxonomic range for this enzyme is: Thermococcus

EC NUMBER
COMMENTARY
1.2.7.5
-
RECOMMENDED NAME
GeneOntology No.
aldehyde ferredoxin oxidoreductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
an aldehyde + H2O + 2 oxidized ferredoxin = a carboxylate + 2 H+ + 2 reduced ferredoxin
show the reaction diagram
-
-
-
-
an aldehyde + H2O + 2 oxidized ferredoxin = a carboxylate + 2 H+ + 2 reduced ferredoxin
show the reaction diagram
substrate binding, catalytic site and reaction mechanism including cofactor action
-
an aldehyde + H2O + 2 oxidized ferredoxin = a carboxylate + 2 H+ + 2 reduced ferredoxin
show the reaction diagram
active site structure
-
an aldehyde + H2O + 2 oxidized ferredoxin = a carboxylate + 2 H+ + 2 reduced ferredoxin
show the reaction diagram
active site structure; intermolecular interaction analysis; substrate binding, catalytic site and reaction mechanism including cofactor action
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Glycolysis / Gluconeogenesis
-
Metabolic pathways
-
Microbial metabolism in diverse environments
-
Pentose phosphate pathway
-
SYSTEMATIC NAME
IUBMB Comments
aldehyde:ferredoxin oxidoreductase
This is an oxygen-sensitive enzyme that contains tungsten-molybdopterin and iron-sulfur clusters. Catalyses the oxidation of aldehydes (including crotonaldehyde, acetaldehyde, formaldehyde and glyceraldehyde) to their corresponding acids. However, it does not oxidize glyceraldehyde 3-phosphate [see EC 1.2.7.6, glyceraldehyde-3-phosphate dehydrogenase (ferredoxin)]. Can use ferredoxin or methyl viologen but not NAD(P)+ as electron acceptor.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
aldehyde ferredoxin oxidoreductase
-
-
aldehyde ferredoxin oxidoreductase
Magnetospirillum magneticum AMB-1.
-
-
-
aldehyde oxidase (ferredoxin)
-
-
-
-
aldehyde oxidoreductase
-
-
aldehyde oxidoreductase
Desulfovibrio aminophilus DSM12254
-
-
-
AOR
-
-
-
-
AOR
Desulfovibrio aminophilus DSM12254
-
-
-
oxidase, aldehyde (ferredoxin)
-
-
-
-
POR
Pyrococcus furiosus DSM3638
-
-
-
formaldehyde ferredoxin oxidoreductase
Q8U1K3
-
additional information
-
formaldehyde ferredoxin oxidoreductase and aldehyde ferredoxin oxidoreductase are 2 separate enzymes
CAS REGISTRY NUMBER
COMMENTARY
138066-90-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain DSM12254
-
-
Manually annotated by BRENDA team
Desulfovibrio aminophilus DSM12254
strain DSM12254
-
-
Manually annotated by BRENDA team
strain AMB-1. The non-magnetic mutant, NMA21 is defective in aldehyde ferredoxin oxidoreductase gene
-
-
Manually annotated by BRENDA team
Magnetospirillum magneticum AMB-1.
strain AMB-1. The non-magnetic mutant, NMA21 is defective in aldehyde ferredoxin oxidoreductase gene
-
-
Manually annotated by BRENDA team
contains a formaldehyde and an aldehyde ferredoxin oxidoreductase; genes aor and for; hyperthermophilic archaeon; strain DSM 3638
-
-
Manually annotated by BRENDA team
contains a formaldehyde and an aldehyde ferredoxin oxidoreductase; hyperthermophilic archaeon; Protein Data Bank entries 1B25 and 1B4N
-
-
Manually annotated by BRENDA team
contains a formaldehyde and an aldehyde ferredoxin oxidoreductase; hyperthermophilic archaeon; strain DSM 3638
-
-
Manually annotated by BRENDA team
gene aor; hyperthermophilic archaeon; strain DSM 3638
SwissProt
Manually annotated by BRENDA team
hyperthermophilic archaeon
-
-
Manually annotated by BRENDA team
hyperthermophilic archaeon; strain DSM 3638
-
-
Manually annotated by BRENDA team
hyperthermophilic archaeon
-
-
Manually annotated by BRENDA team
formaldehyde ferredoxin oxidoreductase; hyperthermophilic archaeon
-
-
Manually annotated by BRENDA team
hyperthermophilic archaeon
-
-
Manually annotated by BRENDA team
hyperthermophilic archaeon
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
the enzyme plays a role in peptide fermentation
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
ir
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
ir
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
ir
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
show the reaction diagram
-, Q51739
formaldehyde ferredoxin oxidoreductase
-
ir
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
ir
acetaldehyde + H2O + oxidized benzyl viologen
acetate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
ir
acetaldehyde + H2O + oxidized benzyl viologen
acetate + reduced benzyl viologen
show the reaction diagram
-
at 5% of the activity with crotonaldehyde
-
-
?
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
ir
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
show the reaction diagram
-
best substrate
-
ir
acetaldehyde + H2O + oxidized ferredoxin
acetate + H+ + reduced ferredoxin
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
ir
acetate + H+ + reduced methyl viologen
acetaldehyde + H2O + oxidized methyl viologen
show the reaction diagram
-
very low activity, below pH 6.0
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-, Q51739
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase, C1-C3 aldehydes
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase, C1-C3 aldehydes
-
ir
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
enzyme oxidizes aldehydes generated during amino acid catabolism
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-, Q51739
formaldehyde ferredoxin oxidoreductase, enzyme plays a role in peptide fermentation in hyperthermophilic archaea
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase, enzyme plays a role in peptide fermentation in hyperthermophilic archaea
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
?, ir
benzaldehyde + H2O + oxidized benzyl viologen
benzoic acid + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
ir
benzaldehyde + H2O + oxidized benzyl viologen
benzoic acid + H+ + reduced benzyl viologen
show the reaction diagram
-
no activity
-
-
-
benzaldehyde + H2O + oxidized benzyl viologen
benzoate + reduced benzyl viologen
show the reaction diagram
-
at 149% of the activity with crotonaldehyde
-
-
?
benzaldehyde + H2O + oxidized ferredoxin
benzoic acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
butyraldehyde + H2O + oxidized ferredoxin
butyrate + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
ir
butyraldehyde + H2O + oxidized ferredoxin
butyrate + H+ + reduced ferredoxin
show the reaction diagram
-
low activity, formaldehyde ferredoxin oxidoreductase
-
ir
cinnamaldehyde + H2O + oxidized benzyl viologen
cinnamate + reduced benzyl viologen
show the reaction diagram
-
at 139% of the activity with crotonaldehyde
-
-
?
crotonaldehyde + CoA + 2 oxidized ferredoxin
crotonate + CO2 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
Pyrococcus furiosus, Pyrococcus furiosus DSM3638
-
the ability of the 4Fe-ferredoxin to accept electrons is not absolutely dependent upon Asp14 (of ferredoxin), as this residue can be effectively replaced by Cys. However, the efficiency of electron transfer is compromised if Asp14 is replaced by Ser, or if the 4Fe-cluster is converted to the 3Fe-form, but Asp14 does not appear to offer any kinetic advantage over the expected Cys
-
-
?
crotonaldehyde + H2O + oxidized benzyl viologen
pyruvate + H+ + reduced benzyl viologen
show the reaction diagram
-, Q51739
-
-
-
ir
crotonaldehyde + H2O + oxidized benzyl viologen
pyruvate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
ir
crotonaldehyde + H2O + oxidized benzyl viologen
pyruvate + H+ + reduced benzyl viologen
show the reaction diagram
-
no activity
-
-
-
crotonaldehyde + H2O + oxidized benzyl viologen
pyruvate + H+ + reduced benzyl viologen
show the reaction diagram
-
low activity, formaldehyde ferredoxin oxidoreductase
-
-
ir
crotonaldehyde + H2O + oxidized benzyl viologen
pyruvate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
ir
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
crotonaldehyde + H2O + oxidized benzyl viologen
crotonate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
crotonaldehyde + H2O + oxidized ferredoxin
pyruvate + H+ + reduced ferredoxin
show the reaction diagram
-
best substrate
-
-
ir
crotonaldehyde + H2O + oxidized ferredoxin
crotonate + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
crotonaldehyde + H2O + oxidized ferredoxin
crotonate + reduced ferredoxin
show the reaction diagram
-
utilizes a 7Fe ferredoxin as the putative physiological redox partner, instead of a 4Fe ferredoxin as in Pyrococcus furiosus, 17% of the activity with benzyl viologen
-
-
?
crotonaldehyde + H2O + oxidized methyl viologen
pyruvate + H+ + reduced methyl viologen
show the reaction diagram
-
artifical electron acceptor
-
-
ir
crotonaldehyde + H2O + oxidized methyl viologen
crotonate + H+ + reduced methyl viologen
show the reaction diagram
-
-
-
-
?
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
show the reaction diagram
-, Q51739
formaldehyde ferredoxin oxidoreductase
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
ir
formaldehyde + H2O + oxidized benzyl viologen
formate + reduced benzyl viologen
show the reaction diagram
-
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
ir
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
show the reaction diagram
Q8U1K3
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
show the reaction diagram
-
formaldehyde and aldehyde ferredoxin oxidoreductases
-
ir
formaldehyde + H2O + oxidized methyl viologen
formate + H+ + reduced methyl viologen
show the reaction diagram
-
specific activity is 17% compared to the activity with crotonaldehyde
-
-
?
glutaraldehyde + H2O + oxidized methyl viologen
glutarate + H+ + reduced methyl viologen
show the reaction diagram
-, Q51739
-
-
-
-
glutaric dialdehyde + H2O + oxidized benzyl viologen
?
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
-
ir
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
show the reaction diagram
-
-, involved in glycolysis
-
ir
glyceraldehyde + H2O + oxidized methyl viologen
glycerate + H+ + reduced methyl viologen
show the reaction diagram
-
-
-
ir
glyceraldehyde + H2O + oxidized methyl viologen
glycerate + H+ + reduced methyl viologen
show the reaction diagram
-
very poor substrate
-
-
-
hexanal + H2O + oxidized methyl viologen
hexanoate + H+ + reduced methyl viologen
show the reaction diagram
-
specific activity is 5.7% compared to the activity with crotonaldehyde
-
-
?
indoleacetaldehyde + H2O + oxidized benzyl viologen
indoleacetate + H+ + reduced benzyl viologen
show the reaction diagram
-, Q51739
-
-
-
-
indoleacetaldehyde + H2O + oxidized benzyl viologen
indoleacetate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
ir
indoleacetaldehyde + H2O + oxidized benzyl viologen
indoleacetate + H+ + reduced benzyl viologen
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
-
ir
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
ir
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase, no activity
-
-
-
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
show the reaction diagram
Q51739
formaldehyde ferredoxin oxidoreductase, no activity
-
-
-
phenylacetaldehyde + H2O + oxidized benzyl viologen
phenylacetate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
ir
phenylacetaldehyde + H2O + oxidized benzyl viologen
phenylacetate + H+ + reduced benzyl viologen
show the reaction diagram
-
no activity
-
-
-
phenylpropionaldehyde + H2O + oxidized benzyl viologen
phenylpropanoate + H+ + reduced benzyl viologen
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
-
ir
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
ir
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
ir
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
ir
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
show the reaction diagram
-, Q51739
formaldehyde ferredoxin oxidoreductase
-
ir
propionaldehyde + H2O + oxidized benzyl viologen
propionate + H+ + reduced benzyl viologen
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
ir
propionaldehyde + H2O + oxidized ferredoxin
propionate + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
propionaldehyde + H2O + oxidized ferredoxin
propionate + H+ + reduced ferredoxin
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
ir
salicylaldehyde + H2O + oxidized benzyl viologen
salicylic acid + H+ + reduced benzyl viologen
show the reaction diagram
-
-
-
-
ir
succinic semialdehyde + H2O + oxidized benzyl viologen
succinic acid + H+ + reduced benzyl viologen
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase
-
-
ir
isovalerylaldehyde + H2O + oxidized benzyl viologen
isovalerate + H+ + reduced benzyl viologen
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase, no activity
-
-
-
additional information
?
-
-
enzyme shows an active and an inactive form
-
-
-
additional information
?
-
-
acid reduction is strongly dependent on the overall reduction potential, therfore reverse reaction is only possible with reduced methyl viologen at a low rate
-
-
-
additional information
?
-
-
no oxidizing activity with glyceraldehyde-3-phosphate, glyoxylate, glucose, glucose 6-phosphate, CO, H2, formate, pyruvate, 2-oxoglutarate, NAD(P) is no electron acceptor, no H2 evolution from reduced methyl viologen, no activity with CoA
-
-
-
additional information
?
-
-
the enzyme is expressed under microaerobic conditions. The non-magnetic mutant, NMA21 is defective in aldehyde ferredoxin oxidoreductase gene. The enzyme may contribute to ferric iron reduction during synthesis of bacterial magnetic particles under microaerobic respiration
-
-
-
additional information
?
-
-
no activity towards xanthine, allopurinol, and isoquinoline, inactive towards N-heterolytic compounds
-
-
-
additional information
?
-
-
the enzyme is most active on aldehydes derived from amino acids
-
-
-
additional information
?
-
Magnetospirillum magneticum AMB-1.
-
the enzyme is expressed under microaerobic conditions. The non-magnetic mutant, NMA21 is defective in aldehyde ferredoxin oxidoreductase gene. The enzyme may contribute to ferric iron reduction during synthesis of bacterial magnetic particles under microaerobic respiration
-
-
-
additional information
?
-
Desulfovibrio aminophilus DSM12254
-
no activity towards xanthine, allopurinol, and isoquinoline, inactive towards N-heterolytic compounds
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
enzyme oxidizes aldehydes generated during amino acid catabolism
-
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-, Q51739
formaldehyde ferredoxin oxidoreductase, enzyme plays a role in peptide fermentation in hyperthermophilic archaea
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
formaldehyde ferredoxin oxidoreductase, enzyme plays a role in peptide fermentation in hyperthermophilic archaea
-
?
an aldehyde + H2O + oxidized ferredoxin
an acid + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
show the reaction diagram
Q8U1K3
-
-
-
?
formaldehyde + H2O + oxidized ferredoxin
formate + H+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
glyceraldehyde + H2O + oxidized ferredoxin
glycerate + H+ + reduced ferredoxin
show the reaction diagram
-
involved in glycolysis
-
ir
additional information
?
-
Magnetospirillum magneticum, Magnetospirillum magneticum AMB-1.
-
the enzyme is expressed under microaerobic conditions. The non-magnetic mutant, NMA21 is defective in aldehyde ferredoxin oxidoreductase gene. The enzyme may contribute to ferric iron reduction during synthesis of bacterial magnetic particles under microaerobic respiration
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Ferredoxin
-
formaldehyde ferredoxin oxidoreductase, binding mechanism
-
Ferredoxin
-, Q51739
;
-
Ferredoxin
-
-
-
Ferredoxin
-
-
-
Ferredoxin
-
-
-
form A cofactor
-
in presence of iodine
-
form A cofactor
-
formaldehyde ferredoxin oxidoreductase
-
form B cofactor
-
in absence of iodine
-
tungsten cofactor
-
formaldehyde ferredoxin oxidoreductase
-
tungsten cofactor
-, Q51739
formaldehyde ferredoxin oxidoreductase; pterin ring system; pterin ring system
-
tungsten cofactor
-
pterin ring system
-
tungsten cofactor
-
formaldehyde ferredoxin oxidoreductase; pterin ring system
-
tungsten cofactor
-
pterin ring system
-
tungsten-molybdopterin
-
interaction with of DXXGL(D,C)X motif and Gly341, Asp343, Asp338, Gly492, Cys494, and Asp489; structural coordination of the tungsten by 4 sulfur ligands in the cofactor; tungstopterin center
tungsten-molybdopterin
-
electron and redox properties
tungsten-molybdopterin
-
modeling of the tungsten sites of inactive and active enzyme forms
tungsten-molybdopterin
-
tungstopterin center
tungsten-molybdopterin
-, Q51739
in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues; in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues
tungsten-molybdopterin
-
in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues
molybdopterin
-
-
additional information
-
the active tungsten center is hydrolyzed to the inactive dioxotungsten(VI) center ([WVIO2]2+) in the absence of sulfide
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
0.7 gatoms per subunit
Ca2+
-
0.4 mol per mol of subunit, formaldehyde ferredoxin oxidoreductase
Ca2+
-
binding site, formaldehyde ferredoxin oxidoreductase
Ca2+
-, Q51739
1 Ca2+ per subunit, formaldehyde ferredoxin oxidoreductase
Fe2+
-
contains 1 iron-sulfur cluster [4Fe-4S] per subunit
Fe2+
-
6.6 gatoms per 85000g of protein
Fe2+
-
contains 1 iron-sulfur cluster [4Fe-4S] per subunit
Fe2+
-
contains 1 iron-sulfur cluster [4Fe-4S] per subunit; electron and redox properties of the [4Fe-4S]-centers
Fe2+
-
3.8 gatoms per subunit, formaldehyde ferredoxin oxidoreductase
Fe2+
-
contains 1 iron-sulfur cluster [4Fe-4S] per subunit; the [4Fe-4S]-cluster is coordinated by Cys287 of the formaldehyde ferredoxin oxidoreductase and Asp14 of ferredoxin, structure
Fe2+
-, Q51739
contains 1 additional Fe2+ besides the [4Fe-4S]-cluster; contains 1 iron-sulfur cluster [4Fe-4S] per subunit; in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues; in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues
Fe2+
-
contains 1 iron-sulfur cluster [4Fe-4S] per subunit; in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues
Fe2+
-
two(2Fe-2S) clusters per monomer
Iron
-
contains 3.3 mol Fe per mol of monomer, the enzyme contains a single [4Fe-4S]2+/1+ cluster per monomer
Iron
-
each subunit carries one [4Fe-4S] cubane and a novel tungsten cofactor containing two pterins. A single iron atom bridges between the subunits. The active-site redox chemistry is based on the pterin part of the cofactor
Mg2+
-
1.5 mol per mol of subunit, formaldehyde ferredoxin oxidoreductase
Mg2+
-, Q51739
both enzyme forms; contains 1 Mg-atom per subunit
Mg2+
-
contains 1 Mg-atom per subunit
Molybdenum
-
-
Molybdenum
-
part of a tungsten-molybdopterin cofactor
Molybdenum
-
part of a tungsten-molybdopterin cofactor
Molybdenum
-
molybdenum centre
Tungsten
-
1 tungsten per subunit
Tungsten
-
1.0 gatoms per 85000g of protein; part of a tungsten-molybdopterin cofactor
Tungsten
-
tungstoenzyme
Tungsten
-
electron and redox properties of the 2 tungsten forms with different potential; part of a tungsten-molybdopterin cofactor
Tungsten
-
electron and redox properties of the 2 tungsten forms with different potential
Tungsten
-
part of a tungsten-molybdopterin cofactor
Tungsten
-
0.9 gatom per subunit, formaldehyde ferredoxin oxidoreductase
Tungsten
-, Q51739
1 tungsten per subunit; in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues; in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues
Tungsten
-
in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues
Tungsten
-
1 tungsten per subunit; in each subunit tungsten is coordinated by 4 dithiolene sulfur atoms from 2 pterin molecules, together with a single [4Fe-4S]-cluster coordinated by 4 sulfur atoms from 4 cysteine residues
Tungsten
-
contains 0.7 mol tungsten per mol of monomer, the enzyme contains a single tungstopterin cofactor
Tungsten
-
each subunit carries one [4Fe-4S] cubane and a novel tungsten cofactor containing two pterins. A single iron atom bridges between the subunits
Tungsten
-
the enzyme contains a tungsten oxo-thiolate center, with two W=O at 1.74 A, approximately three W-S ligands at 2.41 A, and (possibly) a W-O or W-N ligand at 2.1 A. The tungsten site of this enzyme is structurally quite similar to that of molybdenum in the molybdenum oxo-thiolate enzymes
Tungsten
-
the enzyme from Pyrococcus furiosus uses exclusively tungsten to synthesize the catalytically active forms of aldehyde ferredoxin oxidoreductase and active molybdenum- or vanadium-containing isoenzymes are not expressed when the cells are grown in the presence of these other metals
Tungsten
Q8U1K3
dependent on
Zn2+
-
0.2 gatoms per subunit
Molybdenum
-
the enzyme with molybdenum has higher redox potential than that with tungsten
additional information
-
contains no detectable molybdenum
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,2'-Bipyridyl
-
competitive to methyl viologen
acetaldehyde
-
50% inhibition at 5 mM
aldehydes
-
substrate inhibition at high concentrations, overview
arsenite
-
50% inhibition at 0.5 mM
arsenite
-
50% inhibition at 1 mM
Crotonaldehyde
-
50% inhibition at 20 mM
Crotonaldehyde
-
substrate inhibition above 0.2 mM
cyanide
-
50% inhibition at 8 mM
iodoacetate
-
50% inhibition at 0.5 mM
iodoacetate
-
50% inhibition at 0.2 mM
p-chloromercuribenzoate
-
-
Phenylacetaldehyde
-
50% inhibition at 7 mM
propionaldehyde
-
50% inhibition at 0.6 mM
Zn2+
-
50% inhibition at 0.25 mM
isovalerylaldehyde
-
50% inhibition at 4 mM
additional information
-
no effect of CoA
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Sulfide
-
activation of formaldehyde ferredoxin oxidoreductase
-
Sulfide
-, Q51739
4-5fold increase in activity at room temperature and pH 8.0 at 20 mM, in presence of 20 mM dithionite; activation of formaldehyde ferredoxin oxidoreductase
-
Tungsten
-, Q51739
stimulates cell growth
Tungsten
-
stimulates cell growth
additional information
-
no effect of CoA
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.016
-
acetaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
60
-
acetaldehyde
-, Q51739
pH 8.4, 85C, benzyl viologen as electron acceptor
1.8
-
acetate
-
pH 8.4, 85C, benzyl viologen as electron acceptor
0.057
-
benzaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
0.17
-
benzyl viologen
-
pH 8.4, 85C, with crotonaldehyde
0.04
-
Crotonaldehyde
-
pH 8.4, 80C, with methyl viologen as electron acceptor
0.13
-
Crotonaldehyde
-
pH 8.4, 45C, benzyl viologen as electron acceptor
0.14
-
Crotonaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
0.3
-
Crotonaldehyde
-
pH 8.4, 60C
0.01
-
Ferredoxin
-
ES-1 ferredoxin; pH 8.4, 85C, with crotonaldehyde
-
1.42
-
formaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
25
-
formaldehyde
-
formaldehyde ferredoxin oxidoreductase, pH 8.4, 80C, with benzyl viologen as electron acceptor
25
-
formaldehyde
Q51739
formaldehyde ferredoxin oxidoreductase, pH 8.4, 80C, with benzyl viologen as electron acceptor
0.8
-
glutaric dialdehyde
-, Q51739
pH 8.4, 80C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
0.2
-
glyceraldehyde
-
pH 8.4, 45C, benzyl viologen as electron acceptor
1
-
glyceraldehyde
-
pH 8.4, 65C, with methyl viologen as electron acceptor
0.05
-
Indoleacetaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
25
-
Indoleacetaldehyde
-, Q51739
pH 8.4, 80C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
0.028
-
isovalerylaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
0.076
-
Phenylacetaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
15
-
phenylpropionaldehyde
-, Q51739
pH 8.4, 80C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
0.15
-
propionaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
60
-
propionaldehyde
-, Q51739
pH 8.4, 80C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
0.065
-
Salicylaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
8
-
Succinic semialdehyde
-, Q51739
pH 8.4, 80C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor
2.9
-
methyl viologen
-
pH 8.4, 85C, with crotonaldehyde
additional information
-
additional information
-
formaldehyde ferredoxin oxidoreductase, Km for several substrates at different concentrations with purified and sulfide-activated enzyme, overview
-
additional information
-
additional information
-
pH 8.0, 80C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
343
-
acetaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
1.6
-
acetate
-
pH 8.4, 85C, benzyl viologen as electron acceptor
720
-
benzaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
250
-
benzyl viologen
-
pH 8.4, 85C, with crotonaldehyde
22
-
Crotonaldehyde
-
pH 8.4, 45C, benzyl viologen as electron acceptor
269
-
Crotonaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
270
-
Ferredoxin
-
ES-1 ferredoxin, pH 8.4, 85C, with crotonaldehyde
-
950
-
formaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
2.8
-
glyceraldehyde
-
pH 8.4, 45C, benzyl viologen as electron acceptor
55
-
Indoleacetaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
272
-
isovalerylaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
62
-
methyl viologen
-
pH 8.4, 85C, with crotonaldehyde
960
-
Phenylacetaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
1100
-
propionaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
13
-
Salicylaldehyde
-
pH 8.4, 85C, benzyl viologen as electron acceptor
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
additional information
-
pH 8.0, 80C, kinetic parameters for the native and mutant forms of Pyrococcus furiosus ferredoxin
0
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
-
-
65C, pH not specified in the publication
42
-
-
purified formaldehyde ferredoxin oxidoreductase
53.6
-
-
purified enzyme, substrate crotonaldehyde with methyl viologen as electron acceptor
238
-
-
purified enzyme
additional information
-
-
formaldehyde ferredoxin oxidoreductase, substrate specificity
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.4
-
-
assay at
8.4
-
-
sharp maximum
8.4
-
-
assay at
8.4
-
Q51739
assay at
8.4
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
10
-
formaldehyde ferredoxin oxidoreductase, activity increases linearly from pH 5.5 to pH 10.0 at 80C
6
10
-
oxidation of acetaldehyde with benzyl viologen as electron acceptor
7
8.4
-
activity increases with increasing pH at increasing temperature, nearly no activity below pH 7.0
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80
-
Q51739
assay at
80
-
-
assay at
85
-
-
assay at
90
-
-
above
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
60
90
-
formaldehyde ferredoxin oxidoreductase, activity increases 4.5fold from 60C to 90C at pH 8.4
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
additional information
-
the enzyme is expressed under microaerobic conditions
Manually annotated by BRENDA team
additional information
Magnetospirillum magneticum AMB-1.
-
the enzyme is expressed under microaerobic conditions
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Magnetospirillum magneticum AMB-1.
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
90000
-
-
gel filtration
105000
-
-
gel filtration
110000
-
-
gel filtration
130000
-
-
gel filtration
134000
-
-
crystal structure
136100
-
-, Q51739
-
200000
-
-
gel filtration
275000
-
-
formaldehyde ferredoxin oxidoreductase, gel filtration
280000
-
-, Q51739
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
2 * 66000, crystal structure
dimer
-, Q51739
; 2 * 67000
dimer
-
2 * 67000, SDS-PAGE
dimer
-
2 * 68000, SDS-PAGE
dimer
Thermococcus sp. ES-1
-
2 * 67000, SDS-PAGE
-
dimer
-
2 * 67000, SDS-PAGE; 2 * 67000, SDS-PAGE
-
homodimer
-
2 * 66630, calculated from sequence
homodimer
-
2 * 100000, SDS-PAGE
homodimer
-
2 * 80000, SDS-PAGE
homodimer
Desulfovibrio aminophilus DSM12254
-
2 * 100000, SDS-PAGE
-
monomer
-
1 * 80000, SDS-PAGE
tetramer
-
4 * 68000, formaldehyde ferredoxin oxidoreductase, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystallization of the 3 different cofactor model complexes: 1. [Et4N]2[WVIO(1,2-dicyanoethylenedithiolate)2], 2. [Et4N]2[WIVO(1,2-dicyanoethylenedithiolate)2], and 3. [Et4N]2[WVIO(S2)(1,2-dicyanoethylenedithiolate)2], X-ray structure determination and analysis
-
formaldehyde ferredoxin oxidoreductase, purified enzyme, modified melting-point capillary method, room temperature under argon atmosphere, protein solution: 55-65 mg/ml, 50 mM Tris-HCl, pH 8.0, 2 mM dithionite, 2 mM DTT, 0.2 M KCl, precipitant solution: 30% v/v glycerol, 20% w/v PEG 4000, 0.1 M sodium citrate, pH 5.6, 0.2 M NaCl, several weeks, X-ray structure determination and analysis
-
X-ray crystal structure determination and analysis
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
-
pure enzyme, 2 mg/ml, 50 mM Tris-HCl, pH 8.0, 2 mM sodium dithionite, 2 mM DTT, 10% v/v glycerol, exposure to air, irreversible loss of 50% activity after 1 min
23
-
-
pure enzyme, 5.2 mg/ml, 50 mM Tris-HCl, pH 8.0, 2 mM sodium dithionite, 2 mM DTT, 10% v/v glycerol, exposure to air, less than 20% remaining activity after 5 min, after 10 additional min 10% residual activity is reached, which stays constant for more than 30 min
80
-
-
formaldehyde ferredoxin oxidoreductase, t1/2: 8 h, in presence of 2 mM dithionite and 2 mM DTT, pH 8.4
80
-
-, Q51739
aldehyde ferredoxin oxidoreductase, t1/2: 15 min; formaldehyde ferredoxin oxidoreductase, t1/2: 6 h
additional information
-
-
the enzyme is thermostable
additional information
-
-
the enzyme is thermostable
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
10% glycerol and 2 mM DTT stabilize during purification
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
aldehyde ferredoxin oxidoreductase, t1/2: 30 min at 23 C
-, Q51739
644691
formaldehyde ferredoxin oxidoreductase, t1/2: 9 h at 23C
-, Q51739
644691
sensitive against O2, dithionite is added to avoid trace contamination with O2 during purification and enzyme assay
-
11938
very sensitive to O2, after 1 h at 60C 3% activity remains, after 1 h at 4C 39% activity remains
-
11935
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-196C, pure enzyme pellet is thawed anaerobically after storage in liquid N2, no loss of activity for several months
-
4c or 23C, pure enzyme, 50 mM Tris-HCl, pH 8.0, 2 mM sodium dithionite, 2 mM DTT, 10% v/v glycerol, loss of 25% activity after 6 h under strict anaerobic conditions
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme from vanadium- and molybdenum-grown cells
-
formaldehyde and aldehyde ferredoxin oxidoreductase; formaldehyde ferredoxin oxidoreductase, highly reducing and strict anaerobic conditions are required
-, Q51739
formaldehyde ferredoxin oxidoreductase, 17fold
-
to homogeneity under strict anaerobic conditions
-
formaldehyde ferredoxin oxidoreductase, highly reducing and strict anaerobic conditions are required
-
about 120fold, to homogeneity
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
in situ generation of oxo-sulfidobis(dithiolene)tungsten(VI) complexes that model the proposed active-site structure for the AOR family of tungsten enzymes. The complexes are characterized by UV-vis, electrospray ionization mass spectrometry, IR, and resonance Raman spectroscopies and are found to mimic the coordination environment including the W=E (E=O, S) bond strengths and hydrolytic reactions of the tungsten center of the AOR family