In enzymology, a beta-pyrazolylalanine synthase (EC 2.5.1.51) is an enzyme that catalyzes the chemical reaction
| beta-pyrazolylalanine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.5.1.51 | ||||||||
| CAS no. | 37290-81-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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- O3-acetyl-L-serine + pyrazole 3-(pyrazol-1-yl)-L-alanine + acetate
Thus, the two substrates of this enzyme are O3-acetyl-L-serine and pyrazole, whereas its two products are 3-(pyrazol-1-yl)-L-alanine and acetate.
This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is O3-acetyl-L-serine:pyrazole 1-(2-amino-2-carboxyethyl)transferase. Other names in common use include beta-(1-pyrazolyl)alanine synthase, beta-pyrazolealanine synthase, beta-pyrazolylalanine synthase (acetylserine), O3-acetyl-L-serine acetate-lyase (adding pyrazole), BPA-synthase, pyrazolealanine synthase, pyrazolylalaninase, and 3-O-acetyl-L-serine:pyrazole 1-(2-amino-2-carboxyethyl)transferase.
References
edit- Murakoshi I, Ikegami F, Hinuma Y, Hanma Y (1984). "Purification and characterization of beta-(pyrazol-1-yl)-L-alanine synthase from Citrullus vulgaris". Phytochemistry. 23 (5): 973–977. doi:10.1016/S0031-9422(00)82594-7.
- Murakoshi I, Ikegami F, Hinuma Y, Hanma Y (1984). "Purification and characterization of L-mimosine synthase from Leucaena leucocephala". Phytochemistry. 23 (9): 1905–1908. doi:10.1016/S0031-9422(00)84938-9.
- Murakoshi I, Kuramoto H, Haginiwa J (1972). "The enzymic synthesis of beta-substituted alanines". Phytochemistry. 11: 177–182. doi:10.1016/S0031-9422(00)89986-0.
- Noji M, Murakoshi I, Saito K (1993). "Evidence for identity of beta-pyrazolealanine synthase with cysteine synthase in watermelon: formation of beta-pyrazole-alanine by cloned cysteine synthase in vitro and in vivo". Biochem. Biophys. Res. Commun. 197 (3): 1111–7. doi:10.1006/bbrc.1993.2592. PMID 8280125.
