Biology:Beta-pyrazolylalanine synthase

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Short description: Class of enzymes
Beta-pyrazolylalanine synthase
Identifiers
EC number2.5.1.51
CAS number37290-81-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Beta-pyrazolylalanine synthase (EC 2.5.1.51) is an enzyme that catalyzes the chemical reaction

  1. REDIRECT Template:Chemical reaction

It was first characterised from Leucaena leucocephala and transfers the 2-amino-2-carboxyethyl group from its substrate, the amino acid O-acetylserine, to pyrazole, giving β-pyrazolyl-L-alanine. Acetic acid (CH
3
CO
2
H
) is a byproduct.[1][2] The enzyme is also found in Citrullus vulgaris (watermelon) and, unlike some other cysteine synthase enzymes which use O-acetylserine, in this species is specific for pyrazole.[3][4]

This enzyme is a transferase, 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.[5]

References

  1. "The enzymic synthesis of beta-substituted alanines". Phytochemistry 11 (1): 177–182. 1972. doi:10.1016/S0031-9422(00)89986-0. Bibcode1972PChem..11..177M. 
  2. "Purification and characterization of L-mimosine synthase from Leucaena leucocephala". Phytochemistry 23 (9): 1905–1908. 1984. doi:10.1016/S0031-9422(00)84938-9. Bibcode1984PChem..23.1905M. 
  3. "Purification and characterization of beta-(pyrazol-1-yl)-L-alanine synthase from Citrullus vulgaris". Phytochemistry 23 (5): 973–977. 1984. doi:10.1016/S0031-9422(00)82594-7. Bibcode1984PChem..23..973M. 
  4. "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. 1993. doi:10.1006/bbrc.1993.2592. PMID 8280125. Bibcode1993BBRC..197.1111N. 
  5. Enzyme 2.5.1.51 at KEGG Pathway Database.