Active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions.
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The Structure- and Metal-dependent Activity of Escherichia coli PgaB Provides Insight into the Partial De-N-acetylation of Poly- -1,6-N-acetyl-D-glucosamineElemental economy: microbial strategies for optimizing growth in the face of nutrient limitation.Genetically encoded ratiometric biosensors to measure intracellular exchangeable zinc in Escherichia coli.ZntR-mediated transcription of zntA responds to nanomolar intracellular free zinc.Structure, inhibition, and regulation of essential lipid A enzymes.The Metal Drives the Chemistry: Dual Functions of Acireductone Dioxygenase.Structural and thermodynamic characterization of metal binding in Vps29 from Entamoeba histolytica: Implication in retromer function.Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of LpxC is conserved in enterobacteria but not in all gram-negative bacteria.Kinetics and thermodynamics of metal-binding to histone deacetylase 8.The activity and cofactor preferences of N-acetyl-1-D-myo-inosityl-2-amino-2-deoxy-alpha-D-glucopyranoside deacetylase (MshB) change depending on environmental conditions.The DNA uptake ATPase PilF of Thermus thermophilus: a reexamination of the zinc content.Identity of cofactor bound to mycothiol conjugate amidase (Mca) influenced by expression and purification conditions.Active Site Metal Identity Alters Histone Deacetylase 8 Substrate Selectivity: A Potential Novel Regulatory Mechanism.Cross-functionalities of Bacillus deacetylases involved in bacillithiol biosynthesis and bacillithiol-S-conjugate detoxification pathways.
P2860
Q27670808-E08FF5B1-FC1F-4A4A-AB0A-A50BEF2A8265Q33911028-6424A20B-CD38-464F-B2D4-058B5B89A35BQ35194380-FE49AC26-6FF0-4E98-8D40-EE34A8B19BC5Q36129920-1F9AB177-E794-40C8-AB78-7596C943428FQ39035338-D93850A4-563A-4A70-9F40-10B611E321B8Q39450455-4FBDAA90-18DB-4377-B7F3-6A2C501CBC92Q40051280-D55FCDBB-7BE9-43DB-8A7D-7572688840A5Q41430702-4BAF8D7C-85D1-42A7-9F87-153280D55175Q41680639-2B32FB92-BC91-48D0-ABB1-E2495F061F5AQ41810835-D63A4F0C-7309-4218-BAE8-FFC16E0A7952Q43018469-65DF99DD-46C2-4614-AF72-49E925D978F8Q45014510-9C653710-12FA-43D3-87FD-423ACC50B530Q47647184-00823D6D-DE4B-4349-AF1E-6E6768701C13Q50915989-CE4C2903-2973-4CEC-8BB7-928847E0BC86
P2860
Active site metal ion in UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase (LpxC) switches between Fe(II) and Zn(II) depending on cellular conditions.
description
2010 nî lūn-bûn
@nan
2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Active site metal ion in UDP-3-O-
@nl
Active site metal ion in UDP-3 ...... ending on cellular conditions.
@ast
Active site metal ion in UDP-3 ...... ending on cellular conditions.
@en
type
label
Active site metal ion in UDP-3-O-
@nl
Active site metal ion in UDP-3 ...... ending on cellular conditions.
@ast
Active site metal ion in UDP-3 ...... ending on cellular conditions.
@en
prefLabel
Active site metal ion in UDP-3-O-
@nl
Active site metal ion in UDP-3 ...... ending on cellular conditions.
@ast
Active site metal ion in UDP-3 ...... ending on cellular conditions.
@en
P2093
P2860
P356
P1476
Active site metal ion in UDP-3 ...... ending on cellular conditions.
@en
P2093
Carol A Fierke
Marcy Hernick
Samuel G Gattis
P2860
P304
33788-33796
P356
10.1074/JBC.M110.147173
P407
P577
2010-08-13T00:00:00Z