Cloned (Comment) | Organism |
---|---|
gene cctP | Talaromyces islandicus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-phenylalanine | Aster tataricus | - |
L-beta-phenylalanine | - |
r | |
L-phenylalanine | Taxus chinensis | - |
L-beta-phenylalanine | - |
r | |
L-phenylalanine | Talaromyces islandicus | - |
L-beta-phenylalanine | - |
r | |
L-phenylalanine | Pelliciarosea asterica | - |
L-beta-phenylalanine | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aster tataricus | - |
- |
- |
Pelliciarosea asterica | - |
- |
- |
Talaromyces islandicus | A0A0U1LSP0 | - |
- |
Taxus chinensis | Q68G84 | i.e. Taxus chinensis | - |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
L-phenylalanine = L-beta-phenylalanine | (R)-selective PAM reaction mechanism, overview | Aster tataricus | |
L-phenylalanine = L-beta-phenylalanine | (R)-selective PAM reaction mechanism, overview | Taxus chinensis | |
L-phenylalanine = L-beta-phenylalanine | (R)-selective PAM reaction mechanism, overview | Talaromyces islandicus | |
L-phenylalanine = L-beta-phenylalanine | (R)-selective PAM reaction mechanism, overview | Pelliciarosea asterica |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-phenylalanine | - |
Aster tataricus | L-beta-phenylalanine | - |
r | |
L-phenylalanine | - |
Taxus chinensis | L-beta-phenylalanine | - |
r | |
L-phenylalanine | - |
Talaromyces islandicus | L-beta-phenylalanine | - |
r | |
L-phenylalanine | - |
Pelliciarosea asterica | L-beta-phenylalanine | - |
r | |
L-phenylalanine | L-alpha-phenylalanine | Aster tataricus | L-beta-phenylalanine | - |
r | |
L-phenylalanine | L-alpha-phenylalanine | Taxus chinensis | L-beta-phenylalanine | - |
r | |
L-phenylalanine | L-alpha-phenylalanine | Talaromyces islandicus | L-beta-phenylalanine | - |
r | |
L-phenylalanine | L-alpha-phenylalanine | Pelliciarosea asterica | L-beta-phenylalanine | - |
r |
Synonyms | Comment | Organism |
---|---|---|
(R)-PAM | - |
Aster tataricus |
(R)-PAM | - |
Taxus chinensis |
(R)-PAM | - |
Talaromyces islandicus |
(R)-PAM | - |
Pelliciarosea asterica |
(R)-selective PAM | - |
Aster tataricus |
(R)-selective PAM | - |
Taxus chinensis |
(R)-selective PAM | - |
Talaromyces islandicus |
(R)-selective PAM | - |
Pelliciarosea asterica |
CctP | - |
Talaromyces islandicus |
PAM | - |
Aster tataricus |
PAM | - |
Taxus chinensis |
PAM | - |
Talaromyces islandicus |
PAM | - |
Pelliciarosea asterica |
phenylalanine-2,3-aminomutase | - |
Aster tataricus |
phenylalanine-2,3-aminomutase | - |
Taxus chinensis |
phenylalanine-2,3-aminomutase | - |
Talaromyces islandicus |
phenylalanine-2,3-aminomutase | - |
Pelliciarosea asterica |
TcPAM | - |
Taxus chinensis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
3,5-dihydro-5-methylidene-4H-imidazol-4-one | i.e. MIO, essential cofactor | Aster tataricus | |
3,5-dihydro-5-methylidene-4H-imidazol-4-one | i.e. MIO, essential cofactor | Taxus chinensis | |
3,5-dihydro-5-methylidene-4H-imidazol-4-one | i.e. MIO, essential cofactor | Talaromyces islandicus | |
3,5-dihydro-5-methylidene-4H-imidazol-4-one | i.e. MIO, essential cofactor | Pelliciarosea asterica |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the MIO-dependent aminomutases. Aminomutases (defined as isomerases mediating intramolecular transfer of amino groups) catalyze the synthetically challenging shift of an amine group along a saturated carbon chain, typically of an amino acid. PAMs and tyrosine aminomutases (TAMs) share the same structure, mechanistic pathway, and characteristics of phenylalanine ammonia-lyases (PALs), histidine ammonia-lyases (HALs), and tyrosine ammonia-lyases (TALs), being all members of the same MIO-dependent enzyme family, also called class I lyase-like enzymes | Aster tataricus |
evolution | the enzyme belongs to the MIO-dependent aminomutases. Aminomutases (defined as isomerases mediating intramolecular transfer of amino groups) catalyze the synthetically challenging shift of an amine group along a saturated carbon chain, typically of an amino acid. PAMs and tyrosine aminomutases (TAMs) share the same structure, mechanistic pathway, and characteristics of phenylalanine ammonia-lyases (PALs), histidine ammonia-lyases (HALs), and tyrosine ammonia-lyases (TALs), being all members of the same MIO-dependent enzyme family, also called class I lyase-like enzymes | Taxus chinensis |
evolution | the enzyme belongs to the MIO-dependent aminomutases. Aminomutases (defined as isomerases mediating intramolecular transfer of amino groups) catalyze the synthetically challenging shift of an amine group along a saturated carbon chain, typically of an amino acid. PAMs and tyrosine aminomutases (TAMs) share the same structure, mechanistic pathway, and characteristics of phenylalanine ammonia-lyases (PALs), histidine ammonia-lyases (HALs), and tyrosine ammonia-lyases (TALs), being all members of the same MIO-dependent enzyme family, also called class I lyase-like enzymes | Talaromyces islandicus |
evolution | the enzyme belongs to the MIO-dependent aminomutases. Aminomutases (defined as isomerases mediating intramolecular transfer of amino groups) catalyze the synthetically challenging shift of an amine group along a saturated carbon chain, typically of an amino acid. PAMs and tyrosine aminomutases (TAMs) share the same structure, mechanistic pathway, and characteristics of phenylalanine ammonia-lyases (PALs), histidine ammonia-lyases (HALs), and tyrosine ammonia-lyases (TALs), being all members of the same MIO-dependent enzyme family, also called class I lyase-like enzymes | Pelliciarosea asterica |
metabolism | phenylalanine aminomutase (PAM) catalyzes the 2,3-shift of the alpha-amino group of L-phenylalanine and L-tyrosine to afford beta-phenylalanine. Biocatalytic strategies for the production of (R)- or (S)-beta-arylalanines employing enzymes with enantiocomplementary aminomutase activity | Pelliciarosea asterica |
metabolism | phenylalanine aminomutase (PAM) catalyzes the 2,3-shift of the alpha-amino group of L-phenylalanine and L-tyrosine to afford beta-phenylalanine. Biocatalytic strategies for the production of (R)- or (S)-beta-arylalanines employing enzymes with enantiocomplementary aminomutase activity. (R)-beta-phenylalanine is a precursor in biosynthesis of taxol in Taxus species | Taxus chinensis |
metabolism | phenylalanine aminomutase (PAM) catalyzes the 2,3-shift of the alpha-amino group of L-phenylalanine and L-tyrosine to afford beta-phenylalanine. Biocatalytic strategies for the production of (R)- or (S)-beta-arylalanines employing enzymes with enantiocomplementary aminomutase activity. Metabolites containing (R)-beta-phenylalanine are chemically similar astins from the plant Aster tataricus | Aster tataricus |
metabolism | phenylalanine aminomutase (PAM) catalyzes the 2,3-shift of the alpha-amino group of L-phenylalanine and L-tyrosine to afford beta-phenylalanine. Biocatalytic strategies for the production of (R)- or (S)-beta-arylalanines employing enzymes with enantiocomplementary aminomutase activity. Metabolites containing (R)-beta-phenylalanine are chemically similar cyclochlorotines from the plant Talaromyces islandicum | Talaromyces islandicus |