The enzymology of cystathionine biosynthesis: strategies for the control of substrate and reaction specificity.
Arch Biochem Biophys
; 433(1): 166-75, 2005 Jan 01.
Article
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| MEDLINE
| ID: mdl-15581575
ABSTRACT
The ability of enzymes to catalyze specific reactions, while excluding others, is central to cellular metabolism. Control of reaction specificity is of particular importance for enzymes that employ catalytically versatile cofactors, of which pyridoxal 5'-phosphate is a prime example. Cystathionine gamma-synthase and cystathionine beta-synthase are the first enzymes in the transsulfuration and reverse transsulfuration pathways, respectively. Each of them occupies branch-point positions in amino acid metabolism and as such are subject to transcriptional and post-translational regulation. Both enzymes catalyze the pyridoxal 5'-phosphate-dependent formation of l-cystathionine; however, their substrate and reaction specificities are distinct. The mechanisms whereby these enzymes control the chemistry of the cofactor are the subject of this review.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Liasas de Carbono-Oxígeno
/
Cistationina
/
Cistationina betasintasa
Idioma:
En
Revista:
Arch Biochem Biophys
Año:
2005
Tipo del documento:
Article