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Information on EC 1.17.98.4 - formate dehydrogenase (hydrogenase)
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1.17.98.4 formate dehydrogenase (hydrogenase)IUBMB Comments
Formate dehydrogenase H is a cytoplasmic enzyme that oxidizes formate without oxygen transfer, transferring electrons to a hydrogenase. The two enzymes form the formate-hydrogen lyase complex . The enzyme contains an [4Fe-4S] cluster, a selenocysteine residue and a molybdopterin cofactor .
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Word Map
- 1.17.98.4
- fhl
- hydrogenases
- nife-hydrogenase
-
formate-dependent
- hycb
-
selenopolypeptide
-
molybdoenzyme
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h2-evolving
-
biohydrogen
-
h2-oxidizing
-
54-dependent
- f0f1-atpase
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Reaction Schemes
+
an [oxidized hydrogenase]
=
+
a [reduced hydrogenase]
Synonyms
formate hydrogenlyase, formate dehydrogenase o, fdhf gene product, benzylviologen-linked formate dehydrogenase, methylviologen-dependent formate dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.1.99.33
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-
formerly
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EC 1.17.99.7
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formerly
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Fdh-H
FDHH
formate dehydrogenase H
formate hydrogenlyase
-
hydrogenase 3 (Hyd-3) together with formate dehydrogenase H (FDH-H) forms part of the formate hydrogenlyase (FHL) complex
Fdh-H
-
hydrogenase 3 (Hyd-3) together with formate dehydrogenase H (FDH-H) forms part of the formate hydrogenlyase (FHL) complex
formate dehydrogenase H
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
formate + an [oxidized hydrogenase] = CO2 + a [reduced hydrogenase]
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-
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SYSTEMATIC NAME
IUBMB Comments
formate:[oxidized hydrogenase] oxidoreductase
Formate dehydrogenase H is a cytoplasmic enzyme that oxidizes formate without oxygen transfer, transferring electrons to a hydrogenase. The two enzymes form the formate-hydrogen lyase complex [1]. The enzyme contains an [4Fe-4S] cluster, a selenocysteine residue and a molybdopterin cofactor [1].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
formate + HycB
CO2 + reduced HycB
-
the hydrogenase 3 Fe-S subunit HycB may represent the electron transfer partner of FDH-H
-
-
?
formate + acceptor
CO2 + reduced acceptor
-
formate dehydrogenase H (FDHH) catalyses the first step in the formate hydrogen lyase (FHL) system
-
-
?
formate + acceptor
CO2 + reduced acceptor
-
the transfer of the formate proton, H+(formate), from formate to the active site base Y- is thermodynamically coupled to two-electron oxidation of the formate molecule, thereby facilitating formation of CO2. Under normal physiological conditions, when electron flow is not limited by the terminal acceptor of electrons, the energy released upon oxidation of Mo(IV) centers by the Fe4S4 is used for deprotonation of YH(formate) and transfer of H+(formate) against the thermodynamic potential. This mechanism of proton release from FDH(Se) may play a physiological role in delivery of the formate proton H+(formate) to hydrogenase 3, which is the natural terminal acceptor of electrons for FDH(Se)
-
-
?
formate + acceptor
CO2 + reduced acceptor
-
the reinterpretation of the crystal structure suggests a new reaction mechanism: In step I, formate binds directly to Mo, displacing Se-Cys140. In step II, the alpha-proton from formate may be transferred to the nearby His141 that acts as general base. In this step the CO2 molecule can be released and two electrons transferred to Mo. Alternatively, step II may involve a selenium-carboxylated intermediate. In step III, electrons from Mo(IV) are transferred via the [4Fe-4S] center to an external electron acceptor and the catalytic cycle is completed
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
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the enzyme may have a role in formate reuptake
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-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
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-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
-
the transfer of the formate proton, H+(formate), from formate to the active site base Y- is thermodynamically coupled to two-electron oxidation of the formate molecule, thereby facilitating formation of CO2. Under normal physiological conditions, when electron flow is not limited by the terminal acceptor of electrons, the energy released upon oxidation of Mo(IV) centers by the Fe4S4 is used for deprotonation of YH(formate) and transfer of H+(formate) against the thermodynamic potential. This mechanism of proton release from FDH(Se) may play a physiological role in delivery of the formate proton H+(formate) to hydrogenase 3, which is the natural terminal acceptor of electrons for FDH(Se)
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
-
FDH-H remains essentially unchanged when deuteroformate is used as a substrate
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-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
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formate oxidation is not rate-limiting in the overall coupled reaction of formate oxidation and benzyl viologen reduction
-
-
?
formate + benzyl viologen
CO2 + reduced benzyl viologen
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ping-pong bi-bi kinetic mechanism
-
-
?
formate + oxidized coenzyme F420
CO2 + reduced coenzyme F420
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-
-
-
?
formate + oxidized coenzyme F420
CO2 + reduced coenzyme F420
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-
-
-
?
additional information
?
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-
Escherichia coli possesses two hydrogenases, Hyd-3 and Hyd-4. These, in conjunction with formate dehydrogenase H (Fdh-H), constitute distinct membrane-associated formate hydrogenlyases, FHL-1 and FHL-2, both catalyzing the decomposition of formate to H2 and CO2 during fermentative growth. FHL-1 is the major pathway at acidic pH. At alkaline pH formate increases an activity of Fdh-H and of Hyd-3 both but not of Hyd-4
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-
?
additional information
?
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-
hydrogenase 3 but not hydrogenase 4 is the major enzyme in hydrogen gas production by Escherichia coli formate hydrogenlyase at acidic pH and in the presence of external formate
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-
?
additional information
?
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physiological role of FSH-O is to ensure rapid adaptation during a shift from aerobiosis to anaerobiosis
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-
?
additional information
?
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the enzyme catalyzes carbon exchange between carbon dioxide and formate in the absence of other electron acceptors, confirming the ping-pong reaction mechanism
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?
additional information
?
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no activity with NADP+ or NAD+
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
formate + benzyl viologen
CO2 + reduced benzyl viologen
-
the enzyme may have a role in formate reuptake
-
-
?
formate + HycB
CO2 + reduced HycB
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the hydrogenase 3 Fe-S subunit HycB may represent the electron transfer partner of FDH-H
-
-
?
formate + acceptor
CO2 + reduced acceptor
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formate dehydrogenase H (FDHH) catalyses the first step in the formate hydrogen lyase (FHL) system
-
-
?
formate + acceptor
CO2 + reduced acceptor
-
the transfer of the formate proton, H+(formate), from formate to the active site base Y- is thermodynamically coupled to two-electron oxidation of the formate molecule, thereby facilitating formation of CO2. Under normal physiological conditions, when electron flow is not limited by the terminal acceptor of electrons, the energy released upon oxidation of Mo(IV) centers by the Fe4S4 is used for deprotonation of YH(formate) and transfer of H+(formate) against the thermodynamic potential. This mechanism of proton release from FDH(Se) may play a physiological role in delivery of the formate proton H+(formate) to hydrogenase 3, which is the natural terminal acceptor of electrons for FDH(Se)
-
-
?
formate + oxidized coenzyme F420
CO2 + reduced coenzyme F420
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-
-
-
?
formate + oxidized coenzyme F420
CO2 + reduced coenzyme F420
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-
-
-
?
additional information
?
-
-
Escherichia coli possesses two hydrogenases, Hyd-3 and Hyd-4. These, in conjunction with formate dehydrogenase H (Fdh-H), constitute distinct membrane-associated formate hydrogenlyases, FHL-1 and FHL-2, both catalyzing the decomposition of formate to H2 and CO2 during fermentative growth. FHL-1 is the major pathway at acidic pH. At alkaline pH formate increases an activity of Fdh-H and of Hyd-3 both but not of Hyd-4
-
-
?
additional information
?
-
-
hydrogenase 3 but not hydrogenase 4 is the major enzyme in hydrogen gas production by Escherichia coli formate hydrogenlyase at acidic pH and in the presence of external formate
-
-
?
additional information
?
-
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physiological role of FSH-O is to ensure rapid adaptation during a shift from aerobiosis to anaerobiosis
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
molybdopterin
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molybdopterin containg enzyme, Mo is coordinated with the Se atom of selenocysteine
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Mo
Se
selenium
-
anaerobic oxidation of formate by Methanococcus vannielii is catalyzed by two readily separable formate dehydrogenases. One of these is a 105000 Da protein that contains molybdenum, iron, and acid-labile sulfide, but not selenium. The other is a high molecular weight complex composed of selenoprotein and molybdo-iron sulfur protein subunits
Fe
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Mo(IV)- and the reduced FeS cluster-containing form of the enzyme is crystallized and this can be converted into Mo(VI)- and oxidized FeS cluster form upon oxidation
Fe
-
oxidation of Mo(IV) centers by the Fe4S4 is used for deprotonation of YH(formate) and transfer of the formate proton H+(formate) against the thermodynamic potential. The Mo-Se bond is estimated to be covalent to the extent of 17-27% of the unpaired electron spin density residing in the valence 4s and 4p selenium orbitals, based on comparison of the scalar and dipolar hyperfine components to atomic 77Se. Two electron oxidation of formate by the Mo(VI) state converts Mo to the reduced Mo(IV) state with the formate proton, H+(formate), transferring to a nearby base Y-. Transfer of one electron to the Fe4S4 center converts Mo(IV) to the EPR detectable Mo(V) state. The Y- is located within magnetic contact to the [Mo-Se] center, as shown by its strong dipolar 1Hf hyperfine couplings. Photolysis of the formate-induced Mo(V) state abolishes the 1Hf hyperfine splitting from YH(formate), suggesting photoisomerization of this group or phototransfer of the proton to a more distant proton acceptor group A-. The minor effect of photolysis on the 77Se-hyperfine interaction with [77Se] selenocysteine suggests that the Y- group is not the Se atom, but instead might be the imidazole ring of the His141 residue which is located in the putative substrate-binding pocket close to the [Mo-Se] center. It is proposed that the transfer of H+(formate) from formate to the active site base Y- is thermodynamically coupled to two-electron oxidation of the formate molecule, thereby facilitating formation of CO2
Fe
-
the reinterpretation of the crystal structure suggests a new reaction mechanism: In step I, formate binds directly to Mo, displacing Se-Cys140. In step II, the alpha-proton from formate may be transferred to the nearby His141 that acts as general base. In this step the CO2 molecule can be released and two electrons transferred to Mo. Alternatively, step II may involve a selenium-carboxylated intermediate. In step III, electrons from Mo(IV) are transferred via the [4Fe-4S] center to an external electron acceptor and the catalytic cycle is completed
Mo
-
enzyme contains a bis-molybdopterin guanine dinucleotide cofactor. EPR spectroscopy of the Mo(V) state indicates a square pyramidal geometry analogous to that of the Mo(IV) center. The strongest ligand field component is likely the single axial Se atom producing a ground orbital configuration Mo(dxy). The Mo-Se bond is estimated to be covalent to the extent of 17-27% of the unpaired electron spin density residing in the valence 4s and 4p selenium orbitals, based on comparison of the scalar and dipolar hyperfine components to atomic 77Se. Two electron oxidation of formate by the Mo(VI) state converts Mo to the reduced Mo(IV) state with the formate proton, H+(formate), transferring to a nearby base Y-. Transfer of one electron to the Fe4S4 center converts Mo(IV) to the EPR detectable Mo(V) state. The Y- is located within magnetic contact to the [Mo-Se] center, as shown by its strong dipolar 1Hf hyperfine couplings. Photolysis of the formate-induced Mo(V) state abolishes the 1Hf hyperfine splitting from YH(formate), suggesting photoisomerization of this group or phototransfer of the proton to a more distant proton acceptor group A-. The minor effect of photolysis on the 77Se-hyperfine interaction with [77Se] selenocysteine suggests that the Y- group is not the Se atom, but instead might be the imidazole ring of the His141 residue which is located in the putative substrate-binding pocket close to the [Mo-Se] center. It is proposed that the transfer of H+(formate) from formate to the active site base Y- is thermodynamically coupled to two-electron oxidation of the formate molecule, thereby facilitating formation of CO2
Mo
-
Mo(IV)- and the reduced FeS cluster-containing form of the enzyme is crystallized and this can be converted into Mo(VI)- and oxidized FeS cluster form upon oxidation
Mo
-
molybdopterin containg enzyme, Mo is coordinated with the Se atom of selenocysteine
Mo
-
the reinterpretation of the crystal structure suggests a new reaction mechanism: In step I, formate binds directly to Mo, displacing Se-Cys140. In step II, the alpha-proton from formate may be transferred to the nearby His141 that acts as general base. In this step the CO2 molecule can be released and two electrons transferred to Mo. Alternatively, step II may involve a selenium-carboxylated intermediate. In step III, electrons from Mo(IV) are transferred via the [4Fe-4S] center to an external electron acceptor and the catalytic cycle is completed
Se
-
formate dehydrogenase H contains selenocysteine as an integral amino acid. Selenium of formate dehydrogenase H is directly involved in formate oxidation
Se
-
Mo of the molybdopterin is coordinated with the Se atom of selenocysteine
Se
-
selenocysteine-containing enzyme. The molybdenum-coordinated selenocysteine is essential for catalytic activity of the native enzyme
Se
-
the enzyme contains selenocysteine. The Mo-Se bond is estimated to be covalent to the extent of 17-27% of the unpaired electron spin density residing in the valence 4s and 4p selenium orbitals, based on comparison of the scalar and dipolar hyperfine components to atomic 77Se. Two electron oxidation of formate by the Mo(VI) state converts Mo to the reduced Mo(IV) state with the formate proton, H+(formate), transferring to a nearby base Y-. Transfer of one electron to the Fe4S4 center converts Mo(IV) to the EPR detectable Mo(V) state. The Y- is located within magnetic contact to the [Mo-Se] center, as shown by its strong dipolar 1Hf hyperfine couplings. Photolysis of the formate-induced Mo(V) state abolishes the 1Hf hyperfine splitting from YH(formate), suggesting photoisomerization of this group or phototransfer of the proton to a more distant proton acceptor group A-. The minor effect of photolysis on the 77Se-hyperfine interaction with [77Se] selenocysteine suggests that the Y- group is not the Se atom, but instead might be the imidazole ring of the His141 residue which is located in the putative substrate-binding pocket close to the [Mo-Se] center. It is proposed that the transfer of H+(formate) from formate to the active site base Y- is thermodynamically coupled to two-electron oxidation of the formate molecule, thereby facilitating formation of CO2
Se
-
the enzyme contains selenocysteine.The trxB gene is required for the formation of selenocysteine containing FDHH polypeptide
Se
-
the fdhF gene of Escherichia coli codes for the selenocysteine-including protein subunit of formate dehydrogenase H
Se
-
the reinterpretation of the crystal structure suggests a new reaction mechanism: In step I, formate binds directly to Mo, displacing Se-Cys140. In step II, the alpha-proton from formate may be transferred to the nearby His141 that acts as general base. In this step the CO2 molecule can be released and two electrons transferred to Mo. Alternatively, step II may involve a selenium-carboxylated intermediate. In step III, electrons from Mo(IV) are transferred via the [4Fe-4S] center to an external electron acceptor and the catalytic cycle is completed
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
N3-
formate oxidation is inhibited strongly and competitively whereas CO2 reduction is inhibited weakly and not competitively; strongly inhibits the oxidation of formate, whereas CO2 reduction is inhibited only weakly and not competitively
NO2-
formate oxidation is inhibited strongly and competitively whereas CO2 reduction is inhibited weakly and not competitively; strongly inhibits the oxidation of formate, whereas CO2 reduction is inhibited only weakly and not competitively
NO3-
formate oxidation is inhibited strongly and competitively whereas CO2 reduction is inhibited weakly and not competitively; strongly inhibits the oxidation of formate, whereas CO2 reduction is inhibited only weakly and not competitively
OCN-
formate oxidation is inhibited strongly and competitively whereas CO2 reduction is inhibited weakly and not competitively; strongly inhibits the oxidation of formate, whereas CO2 reduction is inhibited only weakly and not competitively
SCN-
formate oxidation is inhibited strongly and competitively whereas CO2 reduction is inhibited weakly and not competitively; strongly inhibits the oxidation of formate, whereas CO2 reduction is inhibited only weakly and not competitively
iodoacetamide
-
iodoacetamide-dependent loss of activity occurrs only when formate is present
iodoacetamide
-
addition of 1 mM iodoacetamide, to enzyme preparations in pH 7 buffer containing 2 mM 2-mercaptoethanol inactivates
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
HydN protein
-
the ferredoxin-like proteins HydN and YsaA enhance redox dye-linked activity of the formate dehydrogenase H component of the formate hydrogenlyase complex
-
YsaA protein
-
the ferredoxin-like proteins HydN and YsaA enhance redox dye-linked activity of the formate dehydrogenase H component of the formate hydrogenlyase complex
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
Nitrate reduction to ammonia by enteric bacteria: redundancy, or a strategy for survival during oxygen starvation?
Tuberculosis
Components of the Rv0081-Rv0088 locus encoding a predicted formate hydrogenlyase complex are co-regulated by Rv0081, MprA, and DosR in Mycobacterium tuberculosis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9
formate
-
pH 7.5, 24°C, mutant form of the enzyme in which cysteine replaces selenocysteine
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9
formate
-
pH 7.5, 24°C, mutant form of the enzyme in which cysteine replaces selenocysteine
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.4
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.7
-
pH 6.5: about 40% of maximal activity, pH 9.7: about 40% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
FDH-H synthesis is optimal when Escherichia coli grows fermentatively
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
bound to. The alphabeta catalytic dimer is located in the cytoplasm, with a C-terminal anchor for beta protruding into the periplasm. The gamma subunit, which specifies cytochrome b, crosses the cytoplasmic membrane four times, with the N and C termini exposed to the cytoplasm
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
the enzyme may have a role in formate reuptake
Show AA Sequence and Transmembrane Helices (627 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
105000
-
anaerobic oxidation of formate by Methanococcus vannielii is catalyzed by two readily separable formate dehydrogenases. One of these is a 105000 Da protein that contains molybdenum, iron, and acid-labile sulfide, but not selenium. The other is a high molecular weight complex composed of selenoprotein and molybdo-iron sulfur protein subunits
80000
80000
-
x * 80000, formate dehydrogenase component, the formate-hydrogen lyase complex of Escherichia coli decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. The complex consists of two separable enzymatic activities: a formate dehydrogenase and a hydrogenase, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
-
the FDH-O enzyme complex is composed of three subunits: alpha (FdoG), beta (FdoH) and gamma (FdoI)
?
-
x * 80000, formate dehydrogenase component, the formate-hydrogen lyase complex of Escherichia coli decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. The complex consists of two separable enzymatic activities: a formate dehydrogenase and a hydrogenase, SDS-PAGE
?
-
formate dehydrogenase H (FDH-H) and [NiFe]-hydrogenase 3 (Hyd-3) form the catalytic components of the hydrogen-producing formate hydrogenlyase (FHL) complex
additional information
-
hydrogenase 3 (Hyd-3) together with formate dehydrogenase H (FDH-H) forms part of the formate hydrogenlyase (FHL) complex
additional information
-
hydrogenase 4 (Hyf), in conjunction with formate dehydrogenase H (Fdh-H), forms a respiration-linked proton-translocating formate hydrogenlyase (FHL-2)
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals diffract to 2.6 A resolution and belong to a space group of P4(1)2(1)2 or P4(3)2(1)2 with unit cell dimensions a = b = 146.1 A and c = 82.7 A. There is one monomer of FDH per crystallographic asymmetric unit. Similar diffraction quality crystals of oxidized FDH can be obtained by oxidation of crystals of formate-reduced enzyme with benzyl viologen. Mo(IV)- and the reduced FeS cluster containing form of the enzyme was crystallized and this can be converted into Mo(VI)- and oxidized FeS cluster form upon oxidation
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Sec140Cys
-
mutant enzyme with cysteine substituted at position 140 for the selenocysteine residue has decreased catalytic activity and exhibits a different EPR signal
additional information
-
mutant form of the enzyme in which cysteine replaces selenocysteine. The mutant and wild-type enzymes display similar pH dependencies with respect to activity and stability, although the mutant enzyme profiles are slightly shifted to more alkaline pH. The mutant enzyme binds formate with greater affinity than does the wild-type enzyme, as shown by reduced values of Km and Kd. The mutant enzyme has a turnover number which is more than two orders of magnitude lower than that of the native selenium-containing enzyme. The lower turnover number results from a diminished reaction rate for the initial step of the overall reaction
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme in dilute solutions (30 mg/ml) is rapidly inactivated at basic pH or in the presence of formate under anaerobic conditions, but at higher enzyme concentrations (3 mg/ml) the enzyme is relatively stable
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
high levels of formate dehydrogenase are observed in strain HF only when these cells are grown with formate in the absence of H2. In all strains two- to threefold fluctuations of both hydrogenase and formate dehydrogenase cell-free activities are observed during growth, with peak activities reached in the middle of the exponential phase
high levels of formate dehydrogenase are observed in strain HF only when these cells are grown with formate in the absence of H2. In all strains two- to threefold fluctuations of both hydrogenase and formate dehydrogenase cell-free activities are observed during growth, with peak activities reached in the middle of the exponential phase
-
high levels of formate dehydrogenase are observed in strain HF only when these cells are grown with formate in the absence of H2. In all strains two- to threefold fluctuations of both hydrogenase and formate dehydrogenase cell-free activities are observed during growth, with peak activities reached in the middle of the exponential phase
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Raaijmakers, H.C.; Romao, M.J.
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