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Literature summary for 1.12.98.2 extracted from

  • Lyon, E.J.; Shima, S.; Buurman, G.; Chowdhuri, S.; Batschauer, A.; Steinbach, K.; Thauer, R.K.
    UV-A/blue-light inactivation of the ‘metal-free’ hydrogenase (Hmd) from methanogenic archaea. The enzyme contains functional iron after all (2004), Eur. J. Biochem., 271, 195-204.
    View publication on PubMed
Search for more literature for 1.12.98.2

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Methanocaldococcus jannaschii

General Stability

General Stability Organism
sensitive to UV-A/blue light, CO protects from inactivation Methanocaldococcus jannaschii
sensitive to UV-A/blue light, CO protects from inactivation Methanothermobacter marburgensis

Inhibitors

Inhibitors Comment Organism Structure
CN-
-
 Methanothermobacter marburgensis
CO high concentrations Methanocaldococcus jannaschii
CO high concentrations, reversible Methanothermobacter marburgensis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron enzyme contains iron bound to a cofactor of unknown structure, one iron per monomer, iron is released from cofactor upon light inactivation Methanocaldococcus jannaschii
Iron enzyme contains iron bound to a mercaptoethanol-extractable cofactor of unknown structure, one iron per monomer, iron is released from cofactor upon light inactivation Methanothermobacter marburgensis
additional information no iron-sulfur-cluster or nickel Methanocaldococcus jannaschii
additional information no iron-sulfur-cluster or nickel Methanothermobacter marburgensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
 2 * 40000, SDS-PAGE Methanothermobacter marburgensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5,10-methenyltetrahydromethanopterin + H2 Methanocaldococcus jannaschii involved in methanogenesis 5,10-methylenetetrahydromethanopterin + H+
-
 r
5,10-methenyltetrahydromethanopterin + H2 Methanothermobacter marburgensis involved in methanogenesis 5,10-methylenetetrahydromethanopterin + H+
-
 r

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii
-
-
-
Methanothermobacter marburgensis
-
 DSMZ 2133
-

Oxidation Stability

Oxidation Stability Organism
enzyme is rapidly inactivated upon exposure to oxygen Methanothermobacter marburgensis

Purification (Commentary)

Purification (Comment) Organism
all purification steps are performed in the dark Methanothermobacter marburgensis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
610
-
 purified enzyme, pH 6.0, 40°C, under N2 Methanothermobacter marburgensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5,10-methenyltetrahydromethanopterin + H2
-
 Methanocaldococcus jannaschii 5,10-methylenetetrahydromethanopterin + H+
-
 r
5,10-methenyltetrahydromethanopterin + H2
-
 Methanothermobacter marburgensis 5,10-methylenetetrahydromethanopterin + H+
-
 r
5,10-methenyltetrahydromethanopterin + H2 involved in methanogenesis Methanocaldococcus jannaschii 5,10-methylenetetrahydromethanopterin + H+
-
 r
5,10-methenyltetrahydromethanopterin + H2 involved in methanogenesis Methanothermobacter marburgensis 5,10-methylenetetrahydromethanopterin + H+
-
 r
additional information no reduction of methyl viologen or methyl blue Methanocaldococcus jannaschii ?
-
 ?
additional information no reduction of methyl viologen or methyl blue Methanothermobacter marburgensis ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 40000, SDS-PAGE Methanothermobacter marburgensis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
40 65 2.5-fold higher activity at 65°C than at 40°C Methanothermobacter marburgensis

Cofactor

Cofactor Comment Organism Structure
additional information enzyme contains iron bound to a cofactor of unknown structure Methanocaldococcus jannaschii
additional information enzyme contains iron bound to a mercaptoethanol-extractable cofactor of unknown structure Methanothermobacter marburgensis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.1
-
 CN- pH 6.0, 40°C, under N2, substrate concentration of 0.003 mM Methanothermobacter marburgensis
0.2
-
 CN- pH 6.0, 40°C, under N2, substrate concentration of 0.01 mM Methanothermobacter marburgensis