Cloned (Comment) | Organism |
---|---|
overexpression of a histidine-tagged PhpC fusion protein in Streptomyces lividans | Streptomyces viridochromogenes |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphonoacetaldehyde + NADH + H+ | Streptomyces viridochromogenes | the enzyme catalyzes a step in the phosphinothricin tripeptide pathway | 2-hydroxyethylphosphonate + NAD+ | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces viridochromogenes | - |
DSM 40736 | - |
Purification (Comment) | Organism |
---|---|
- |
Streptomyces viridochromogenes |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
phosphonoacetaldehyde + NADH + H+ | the enzyme catalyzes a step in the phosphinothricin tripeptide pathway | Streptomyces viridochromogenes | 2-hydroxyethylphosphonate + NAD+ | - |
? | |
phosphonoacetaldehyde + NADH + H+ | the reaction proceeds to apparent completion in the presence of NADH, but to a lesser extent with NADPH, which suggests that NADH is the preferred cofactor | Streptomyces viridochromogenes | 2-hydroxyethylphosphonate + NAD+ | - |
? | |
phosphonoacetaldehyde + NADPH + H+ | the reaction proceeds to apparent completion in the presence of NADH, but to a lesser extent with NADPH, which suggests that NADH is the preferred cofactor | Streptomyces viridochromogenes | 2-hydroxyethylphosphonate + NADP+ | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PhpC | - |
Streptomyces viridochromogenes |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Streptomyces viridochromogenes |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.3 | - |
assay at | Streptomyces viridochromogenes |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | the reaction proceeds to apparent completion in the presence of NADH, but to a lesser extent with NADPH, which suggests that NADH is the preferred cofactor | Streptomyces viridochromogenes | |
NADPH | the reaction proceeds to apparent completion in the presence of NADH, but to a lesser extent with NADPH, which suggests that NADH is the preferred cofactor | Streptomyces viridochromogenes |
General Information | Comment | Organism |
---|---|---|
malfunction | the DELTAphpC deletion mutant retains the ability to produce phosphinothricin tripeptide | Streptomyces viridochromogenes |