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Literature summary extracted from

  • Adams, M.W.W.; Mortenson, L.E.
    The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I (1984), J. Biol. Chem., 259, 7045-7055.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.12.7.2 2,2'-bipyridyl 66% activity at 1 mM Clostridium pasteurianum
1.12.7.2 CO hydrogenase I is readily inhibited, hydrogenase II is irreversibly inactivated Clostridium pasteurianum
1.12.7.2 CuSO4 0% activity at 1 mM Clostridium pasteurianum
1.12.7.2 o-phenanthroline 36% activity at 1 mM Clostridium pasteurianum
1.12.7.2 O2 50% activity loss after 2 min Clostridium pasteurianum
1.12.7.2 phenylmethanesulfonyl fluoride 61% activity at 1 mM Clostridium pasteurianum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.12.7.2 0.05
-
 reduced ferredoxin hydrogen evolution, hydrogenase I Clostridium pasteurianum
1.12.7.2 0.05
-
 reduced ferredoxin hydrogenase I, at pH 8.0 and 30°C Clostridium pasteurianum
1.12.7.2 0.13
-
 reduced ferredoxin hydrogen evolution, hydrogenase II Clostridium pasteurianum
1.12.7.2 0.13
-
 reduced ferredoxin hydrogenase II, at pH 8.0 and 30°C Clostridium pasteurianum
1.12.7.2 0.18
-
 oxidized methylene blue hydrogen oxidation, hydrogenase I Clostridium pasteurianum
1.12.7.2 0.18
-
 oxidized methylene blue hydrogenase I, at pH 8.0 and 30°C Clostridium pasteurianum
1.12.7.2 0.31
-
 oxidized methyl viologen hydrogen evolution, hydrogenase II Clostridium pasteurianum
1.12.7.2 0.31
-
 oxidized methyl viologen hydrogenase II, at pH 8.0 and 30°C Clostridium pasteurianum
1.12.7.2 0.4
-
 oxidized methylene blue hydrogen oxidation, hydrogenase II Clostridium pasteurianum
1.12.7.2 0.4
-
 oxidized methylene blue hydrogenase II, at pH 8.0 and 30°C Clostridium pasteurianum
1.12.7.2 5
-
 oxidized methyl viologen hydrogen oxidation, hydrogenase I Clostridium pasteurianum
1.12.7.2 5
-
 oxidized methyl viologen hydrogenase I, at pH 8.0 and 30°C Clostridium pasteurianum
1.12.7.2 5.7
-
 oxidized methyl viologen hydrogen oxidation, hydrogenase II Clostridium pasteurianum
1.12.7.2 5.7
-
 oxidized methyl viologen hydrogenase II, at pH 8.0 and 30°C Clostridium pasteurianum
1.12.7.2 6.25
-
 oxidized methyl viologen hydrogen evolution, hydrogenase I Clostridium pasteurianum
1.12.7.2 6.25
-
 oxidized methyl viologen hydrogenase I, at pH 8.0 and 30°C Clostridium pasteurianum

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.12.7.2 Fe hydrogenase I contains 12 atoms per mol enzyme and hydrogenase II 8 atoms per mol enzyme Clostridium pasteurianum

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.12.7.2 H2 + oxidized ferredoxin Clostridium pasteurianum
-
 H+ + reduced ferredoxin
-
 r
1.12.7.2 H2 + oxidized ferredoxin Clostridium pasteurianum W5
-
 H+ + reduced ferredoxin
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.12.7.2 Clostridium pasteurianum
-
-
-
1.12.7.2 Clostridium pasteurianum
-
 hydrogenase II, uptake hydrogenase
-
1.12.7.2 Clostridium pasteurianum
-
 hydrogenase I, bidirectional hydrogenase
-
1.12.7.2 Clostridium pasteurianum W5
-
-
-

Storage Stability

EC Number Storage Stability Organism
1.12.7.2 -180°C, 4 months, 100% activity Clostridium pasteurianum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.12.7.2 H+ + reduced ferredoxin
-
 Clostridium pasteurianum H2 + oxidized ferredoxin
-
 r
1.12.7.2 H+ + reduced methyl viologen
-
 Clostridium pasteurianum H2 + oxidized methyl viologen
-
 r
1.12.7.2 H2 + electron acceptor methylene blue as electron acceptor Clostridium pasteurianum H+ + reduced electron acceptor
-
 ?
1.12.7.2 H2 + electron acceptor methyl viologen as electron acceptor Clostridium pasteurianum H+ + reduced electron acceptor
-
 ?
1.12.7.2 H2 + electron acceptor methylene blue as electron acceptor Clostridium pasteurianum W5 H+ + reduced electron acceptor
-
 ?
1.12.7.2 H2 + electron acceptor methyl viologen as electron acceptor Clostridium pasteurianum W5 H+ + reduced electron acceptor
-
 ?
1.12.7.2 H2 + oxidized ferredoxin
-
 Clostridium pasteurianum H+ + reduced ferredoxin
-
 r
1.12.7.2 H2 + oxidized ferredoxin
-
 Clostridium pasteurianum W5 H+ + reduced ferredoxin
-
 r
1.12.7.2 H2 + oxidized methyl viologen
-
 Clostridium pasteurianum H+ + reduced methyl viologen
-
 r
1.12.7.2 H2 + oxidized methyl viologen
-
 Clostridium pasteurianum W5 H+ + reduced methyl viologen
-
 r
1.12.7.2 H2 + oxidized methylene blue
-
 Clostridium pasteurianum H+ + reduced methylene blue
-
 r
1.12.7.2 H2 + oxidized methylene blue
-
 Clostridium pasteurianum W5 H+ + reduced methylene blue
-
 r

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.12.7.2 5.8
-
 hydrogen evolution, hydrogenase II Clostridium pasteurianum
1.12.7.2 6.3
-
 hydrogen evolution, hydrogenase I Clostridium pasteurianum
1.12.7.2 7
-
 hydrogenase II, hydrogen oxidation, methylene blue as electron acceptor Clostridium pasteurianum
1.12.7.2 9.1
-
 hydrogen evolution, hydrogenase II Clostridium pasteurianum
1.12.7.2 9.8
-
 hydrogenase I, hydrogen oxidation Clostridium pasteurianum
1.12.7.2 10.5
-
 hydrogenase II, hydrogen oxidation, methylene blue as electron acceptor Clostridium pasteurianum