From Wikipedia, the free encyclopedia
pyrazolylalanine synthase
Identifiers
EC no. 4.2.1.50
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
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme pyrazolylalanine synthase ( EC 4.2.1.50) catalyzes the chemical reaction

L-serine + pyrazole 3-(pyrazol-1-yl)-L-alanine + H2O

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-serine hydro-lyase [adding pyrazole 3-(pyrazol-1-yl)-L-alanine-forming]. Other names in common use include β-pyrazolylalaninase, β-(1-pyrazolyl)alanine synthase, and L-serine hydro-lyase (adding pyrazole). It employs one cofactor, pyridoxal phosphate.

References

  • Dunnill PM, Fowden L (1963). "The biosynthesis of beta-pyrazol-1-ylalanine". J. Exp. Bot. 14: 237–248. doi: 10.1093/jxb/14.2.237.


From Wikipedia, the free encyclopedia
pyrazolylalanine synthase
Identifiers
EC no. 4.2.1.50
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
Search
PMC articles
PubMed articles
NCBI proteins

The enzyme pyrazolylalanine synthase ( EC 4.2.1.50) catalyzes the chemical reaction

L-serine + pyrazole 3-(pyrazol-1-yl)-L-alanine + H2O

This enzyme belongs to the family of lyases, specifically the hydro-lyases, which cleave carbon-oxygen bonds. The systematic name of this enzyme class is L-serine hydro-lyase [adding pyrazole 3-(pyrazol-1-yl)-L-alanine-forming]. Other names in common use include β-pyrazolylalaninase, β-(1-pyrazolyl)alanine synthase, and L-serine hydro-lyase (adding pyrazole). It employs one cofactor, pyridoxal phosphate.

References

  • Dunnill PM, Fowden L (1963). "The biosynthesis of beta-pyrazol-1-ylalanine". J. Exp. Bot. 14: 237–248. doi: 10.1093/jxb/14.2.237.



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