Any feedback?
Literature summary for 1.12.98.1 extracted from
- Purification and characterization of an 8-hydroxy-5-deazaflavin-reducing hydrogenase from the archaebacterium Methanococcus voltae (1987), Eur. J. Biochem., 169, 571-577.
General Stability
| General Stability | Organism |
|---|---|
| FAD stabilizes F420-linked activity against heat inactivation, generally stabilizing | Methanococcus voltae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.016 | - |
coenzyme F420 | - |
Methanococcus voltae |  |
| 1.2 | - |
methyl viologen | - |
Methanococcus voltae | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| soluble | - |
Methanococcus voltae | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | - |
Methanococcus voltae | |
| Nickel | - |
Methanococcus voltae | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 105000 | - |
smallest active species, gel filtration, sucrose density centrifugation | Methanococcus voltae |
| 745000 | - |
gel filtration, sucrose density centrifugation | Methanococcus voltae |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| H2 + coenzyme F420 | Methanococcus voltae | enzyme of methanogenesis pathway | reduced coenzyme F420 | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanococcus voltae | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Methanococcus voltae |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 10 | - |
purified enzyme, F420-linked activity | Methanococcus voltae |
| 50 | - |
purified enzyme, methyl viologen-linked activity | Methanococcus voltae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| H2 + coenzyme F420 | - |
Methanococcus voltae | reduced coenzyme F420 | - |
? | |
| H2 + coenzyme F420 | enzyme of methanogenesis pathway | Methanococcus voltae | reduced coenzyme F420 | - |
? | |
| H2 + methyl viologen | binding site for methyl viologen different from F420 binding site as determined by blocking of binding site with antibodies against native enzyme | Methanococcus voltae | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| multimer | alpha,beta,gamma,delta 55000 + 45000 + 37000 + 27000, SDS-PAGE, exact subunit composition not known, function of delta subunit not known | Methanococcus voltae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
- |
Methanococcus voltae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 65 | - |
methyl viologen-reducing activity heat resistent up to 65°C, F420-reducing activity 75% inactivated at 65°C | Methanococcus voltae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 17.5 | - |
coenzyme F420 | - |
Methanococcus voltae | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
F420 reduction | Methanococcus voltae |
| 7.5 | - |
methyl viologen reduction | Methanococcus voltae |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | 1 mol FAD per mol 105000 Da species | Methanococcus voltae | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
