Literature summary extracted from
Yin, X.; McPhail, K.L., Kim, K.J.; Zabriskie, T.M.
Formation of the nonproteinogenic amino acid 2S,3R-capreomycidine by VioD from the viomycin biosynthesis pathway (2004), Chembiochem, 5, 1278-1281.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
4.2.1.145 |
cloned into the Escherichia coli expression vector pET28a encoding a N-terminal His6-tag |
Streptomyces vinaceus |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
4.2.1.145 |
(2S,3S)-3-hydroxyarginine |
Streptomyces vinaceus |
the enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin |
(2S,3R)-capreomycidine |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.2.1.145 |
Streptomyces vinaceus |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
4.2.1.145 |
- |
Streptomyces vinaceus |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
4.2.1.145 |
(2S,3S)-3-hydroxyarginine |
the enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin |
Streptomyces vinaceus |
(2S,3R)-capreomycidine |
- |
? |
|
4.2.1.145 |
(2S,3S)-3-hydroxyarginine |
the enzyme catalyzes an intramolecular beta-replacement/elimination reaction. VioD is completely stereospecific for (3S)-hydroxy-L-Arg, as no product formation is observed when (3R)-hydroxy-L-Arg is evaluated as substrate |
Streptomyces vinaceus |
(2S,3R)-capreomycidine |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
4.2.1.145 |
VioD |
ambiguous |
Streptomyces vinaceus |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
4.2.1.145 |
30 |
- |
assay at |
Streptomyces vinaceus |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
4.2.1.145 |
7 |
- |
assay at |
Streptomyces vinaceus |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
4.2.1.145 |
pyridoxal 5'-phosphate |
pyridoxal 5'-phosphate dependent enzyme. It is not known if the cofactor is covalently bound to VioD through a lysyl imine, as is common with many PLP-dependent enzymes |
Streptomyces vinaceus |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
4.2.1.145 |
physiological function |
the enzyme is involved in the biosynthesis of the cyclic pentapeptide antibiotic viomycin |
Streptomyces vinaceus |