Purification, crystallization and preliminary crystallographic analysis of the full-length cystathionine β-synthase from Apis mellifera.

ABSTRACT: Cystathionine β-synthase (CBS) is a pyridoxal-5'-phosphate-dependent enzyme that catalyzes the first step of the transsulfuration pathway, namely the condensation of serine with homocysteine to form cystathionine. Mutations in the CBS gene are the single most common cause of hereditary homocystinuria, a multisystemic disease affecting to various extents the vasculature, connective tissues and central nervous system. At present, the crystal structure of CBS from Drosophila melanogaster is the only available structure of the full-length enzyme. Here we describe a cloning, overexpression, purification and preliminary crystallographic analysis of a full-length CBS from Apis mellifera (AmCBS) which maintains 51 and 46% sequence identity with its Drosophila and human homologs, respectively. The

SUBMITTER: Oyenarte I 

PROVIDER: S-EPMC3515373 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature