1.12.5.1: hydrogen:quinone oxidoreductase

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For detailed information about hydrogen:quinone oxidoreductase, go to the full flat file.

Reaction

Synonyms

EC 1.12.99.3, HydABC, hydrogen:menaquinone oxidoreductase, Hydrogen:quinone oxidoreductase, hydrogenase (Wolinella succinogenes clone pHyd1 gene hydA subunit precursor reduced), hydrogenase (Wolinella succinogenes clone pHyd1 gene hydB subunit precursor reduced), hydrogenase (Wolinella succinogenes clone pHyd1 gene hydC subunit)

ECTree

     1 Oxidoreductases

         1.12 Acting on hydrogen as donor

             1.12.5 With a quinone or similar compound as acceptor

                1.12.5.1 hydrogen:quinone oxidoreductase

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Results	in table
486	AA Sequence
4	CAS Registry Number
2	Cloned(Commentary)
3	Cofactor
2	Inhibitors
2	Localization
4	Metals/Ions
12	Molecular Weight [Da]
5	Organism
3	Pathway
16	PDB ID
1	pI Value
11	Protein Variants
3	Purification (Commentary)
1	Reaction
3	Reaction Type
5	Reference
2	Specific Activity [micromol/min/mg]
7	Substrates and Products (Substrate)
5	Subunits
7	Synonyms
1	Systematic Name

Engineering

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Engineering on EC 1.12.5.1 - hydrogen:quinone oxidoreductase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

H122A

Wolinella succinogenes

-

mutation in HydC subunit results in an enzyme with wild-type properties

676044

H158A

Wolinella succinogenes

-

mutation in HydC subunit results in an enzyme with wild-type properties

676044

H186A

Wolinella succinogenes

-

mutation in the HydC subunit causes the loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

676044

H186M

Wolinella succinogenes

-

mutation in the HydC subunit causes the loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

676044

H187A

Wolinella succinogenes

-

mutation in HydC subunit results in an enzyme with wild-type properties

676044

H188A

Wolinella succinogenes

-

mutation in hydA subuni causes loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

676044

H25A

Wolinella succinogenes

-

mutation in the HydC subunit causes the loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

676044

H25M

Wolinella succinogenes

-

mutation in the HydC subunit causes the loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

676044

H305M

Wolinella succinogenes

-

mutation in hydA subuni causes loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

676044

H67A

Wolinella succinogenes

-

mutation in the HydC subunit causes the loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

676044

H67M

Wolinella succinogenes

-

mutation in the HydC subunit causes the loss of quinone reactivity of the hydrogenase, while the activity of benzylviologen reduction is retained. The corresponding mutants do not grow with H2 as electron donor and either fumarate or polysulfide as terminal electron acceptor. The mutants grown with formate and fumarate do not catalyse electron transport from H2 to fumarate or to polysulfide, or quinone reduction by H2, in contrast to the wild-type strain. Cytochrome b is not reduced by H2 in the Triton X-100 extract of the mutant membranes, which contains wild-type amounts of the mutated HydC protein

676044