The dehydratase activity of lacticin 481 synthetase is highly processive
about
Discovery and in vitro biosynthesis of haloduracin, a two-component lantibiotic.Production of dehydroamino acid-containing peptides by Lactococcus lactis.The leader peptide is not required for post-translational modification by lacticin 481 synthetase.Rings, radicals, and regeneration: the early years of a bioorganic laboratoryMutants of the zinc ligands of lacticin 481 synthetase retain dehydration activity but have impaired cyclization activity.Mechanistic investigations of the dehydration reaction of lacticin 481 synthetase using site-directed mutagenesis.The importance of the leader sequence for directing lanthionine formation in lacticin 481.Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds.Enzymatic Halogenation and Dehalogenation Reactions: Pervasive and Mechanistically Diverse.Production of a class II two-component lantibiotic of Streptococcus pneumoniae using the class I nisin synthetic machinery and leader sequence.Mechanistic dissection of the enzyme complexes involved in biosynthesis of lacticin 3147 and nisin.Mechanistic Investigations of PoyD, a Radical S-Adenosyl-l-methionine Enzyme Catalyzing Iterative and Directional Epimerizations in Polytheonamide A Biosynthesis.Mechanism of a Class C Radical S-Adenosyl-l-methionine Thiazole Methyl Transferase.Identification of essential catalytic residues of the cyclase NisC involved in the biosynthesis of nisin.
P2860
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P2860
The dehydratase activity of lacticin 481 synthetase is highly processive
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
The dehydratase activity of lacticin 481 synthetase is highly processive
@en
type
label
The dehydratase activity of lacticin 481 synthetase is highly processive
@en
prefLabel
The dehydratase activity of lacticin 481 synthetase is highly processive
@en
P2860
P356
P1476
The dehydratase activity of lacticin 481 synthetase is highly processive
@en
P2093
Leah M Miller
Neil L Kelleher
P2860
P304
P356
10.1021/JA057203D
P407
P577
2006-02-01T00:00:00Z