Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity

Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity

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http://www.wikidata.org/entity/Q27644399
Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate modeling and active site mutationsMechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structuresAdaptive protein evolution grants organismal fitness by improving catalysis and flexibilityStructural Insights into the Subclass B3 Metallo- -Lactamase SMB-1 and the Mode of Inhibition by the Common Metallo- -Lactamase Inhibitor MercaptoacetateOvercoming differences: The catalytic mechanism of metallo-β-lactamasesTrapping and characterization of a reaction intermediate in carbapenem hydrolysis by B. cereus metallo-beta-lactamase.Characteristics and function of sulfur dioxygenase in Echiuran worm Urechis unicinctusBiapenem inactivation by B2 metallo β-lactamases: energy landscape of the hydrolysis reaction.Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.Engineered mononuclear variants in Bacillus cereus metallo-beta-lactamase BcII are inactive.Common mechanistic features among metallo-beta-lactamases: a computational study of Aeromonas hydrophila CphA enzyme.A variety of roles for versatile zinc in metallo-β-lactamases.Structure of PhnP, a phosphodiesterase of the carbon-phosphorus lyase pathway for phosphonate degradation.AIM-1: An Antibiotic-Degrading Metallohydrolase That Displays Mechanistic Flexibility.Hydrolysis of cephalexin and meropenem by New Delhi metallo-β-lactamase: the substrate protonation mechanism is drug dependent.On the active site of mononuclear B1 metallo β-lactamases: a computational study
P2860

Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity

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http://www.wikidata.org/entity/Q27644399
description
2007 nî lūn-bûn
@nan
2007 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
name
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
@ast
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
@en
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
@nl
type
label
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
@ast
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
@en
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
@nl
prefLabel
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
@ast
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
@en
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698