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Literature summary for 5.4.3.10 extracted from
- ; Weise, N.J.; Ahmed, S.T.; Turner, N.J. Synthetic and therapeutic applications of ammonia-lyases and aminomutases (2018), Chem. Rev., 118, 73-118 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene cctP | Talaromyces islandicus |
Natural Substrates/ Products (Substrates)
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aster tataricus | - |
- |
- |
| Pelliciarosea asterica | - |
- |
- |
| Talaromyces islandicus | A0A0U1LSP0 | - |
- |
| Taxus chinensis | Q68G84 | i.e. Taxus chinensis | - |
Reaction
| 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 and Products (Substrate)
| 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
| 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
| 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
| 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 |
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