Mutation analysis of the histidine residues in the glycylglycine endopeptidase ALE-1.
about
A Novel Trans Conformation of Ligand-Free CalmodulinResidue histidine 669 is essential for the catalytic activity of Bacillus anthracis lethal factor.High resolution structure of an M23 peptidase with a substrate analogue.Shared catalysis in virus entry and bacterial cell wall depolymerization.Identification and structural characterization of LytU, a unique peptidoglycan endopeptidase from the lysostaphin family.Bacillus subtilis CwlP of the SP-{beta} prophage has two novel peptidoglycan hydrolase domains, muramidase and cross-linkage digesting DD-endopeptidase.Surface sensing in Vibrio parahaemolyticus triggers a programme of gene expression that promotes colonization and virulence.
P2860
Q27676149-335A9907-F7A3-44D9-83BD-AEBF20C3B672Q34192622-0ACFB2A0-2321-45B1-8564-8791AC642D61Q36123695-2C4F5A3E-344D-4C5A-BBD3-15FC63E5FE0AQ37161434-98AD45F0-55FE-4A66-A99C-09BB5EF01414Q40125665-8A8B46D7-1A5F-408D-9E31-BD5C8934E519Q41465809-61910BD8-4873-4B20-906C-156FFB2EF983Q41954202-B61C1F92-7EF0-4D54-BCF4-2C75693203B9
P2860
Mutation analysis of the histidine residues in the glycylglycine endopeptidase ALE-1.
description
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name
Mutation analysis of the histidine residues in the glycylglycine endopeptidase ALE-1.
@en
type
label
Mutation analysis of the histidine residues in the glycylglycine endopeptidase ALE-1.
@en
prefLabel
Mutation analysis of the histidine residues in the glycylglycine endopeptidase ALE-1.
@en
P2093
P2860
P1476
Mutation analysis of the histidine residues in the glycylglycine endopeptidase ALE-1.
@en
P2093
Hidekazu Suginaka
Hitoshi Komatsuzawa
Masaru Ohara
Motoyuki Sugai
Tamaki Fujiwara
Tetsuya Nishida
P2860
P304
P356
10.1128/JB.187.2.480-487.2005
P577
2005-01-01T00:00:00Z