Structural highlights
Function
RIZA_BACIU Catalyzes the synthesis of Arg-Xaa dipeptides in an ATP-dependent manner. Has strict specificity toward arginine as the N-terminal substrate.[1]
Publication Abstract from PubMed
RizA is an L-amino-acid ligase from Bacillus subtilis that participates in the biosynthesis of rhizocticin, an oligopeptide antibiotic. The substrate-free form of RizA has been crystallized and the structure was solved at 2.8 A resolution. The amino-acid-binding site appears to be capable of accommodating multiple amino acids, consistent with previous biochemical studies.
Structure of RizA, an L-amino-acid ligase from Bacillus subtilis.,Kagawa W, Arai T, Ishikura S, Kino K, Kurumizaka H Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1125-30. doi:, 10.1107/S2053230X15012698. Epub 2015 Aug 25. PMID:26323296[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kino K, Kotanaka Y, Arai T, Yagasaki M. A novel L-amino acid ligase from Bacillus subtilis NBRC3134, a microorganism producing peptide-antibiotic rhizocticin. Biosci Biotechnol Biochem. 2009 Apr 23;73(4):901-7. PMID:19352016 doi:10.1271/bbb.80842
- ↑ Kagawa W, Arai T, Ishikura S, Kino K, Kurumizaka H. Structure of RizA, an L-amino-acid ligase from Bacillus subtilis. Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1125-30. doi:, 10.1107/S2053230X15012698. Epub 2015 Aug 25. PMID:26323296 doi:http://dx.doi.org/10.1107/S2053230X15012698
