Post-translational modification of polyketide and nonribosomal peptide synthases
β Scribed by Christopher T Walsh; Amy M Gehring; Paul H Weinreb; Luis EN Quadri; Roger S Flugel
- Publisher
- Elsevier Science
- Year
- 1997
- Tongue
- English
- Weight
- 719 KB
- Volume
- 1
- Category
- Article
- ISSN
- 1367-5931
No coin nor oath required. For personal study only.
β¦ Synopsis
The past year has witnessed a major advance in the study of polyketide and nonribosomal peptide biosynthesis with the identification of the phosphopantetheinyl transferase enzyme family, enzymes required to produce active, post-translationally modified polyketide and peptide synthases. Phosphopantetheinyl transferases required for fatty acid, peptide and siderophore biosynthesis have been characterized and a consensus sequence noted in order to facilitate future identification of additional proteins catalyzing phosphopantetheinyl transfer.
π SIMILAR VOLUMES
Prostaglandin D2 synthase (PGDS) (beta-trace protein) is a highly abundant cerebrospinal fluid (CSF) glycoprotein. A number of studies have been performed to determine the potential value of this protein for the diagnosis of various neurological disorders. The measurement of total PGDS levels in CSF