Hsp31 of Escherichia coli K-12 is glyoxalase III. (Q34194675)

31 July 2017

title

Hsp31 of Escherichia coli K-12 is glyoxalase III. (English)

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31 July 2017

main subject

glyoxalase III activity

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Gene Ontology release 2020-05-02

Gene Ontology ID

GO:0019172

Escherichia coli K-12

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author name string

Krishna P Subedi

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31 July 2017

Dongwook Choi

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31 July 2017

Insook Kim

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31 July 2017

Bumchan Min

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31 July 2017

Chankyu Park

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31 July 2017

language of work or name

English

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publication date

6 July 2011

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31 July 2017

published in

Molecular Microbiology

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31 July 2017

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31 July 2017

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31 July 2017

page(s)

926-936

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Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue

31 July 2017

cites work

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104 Methylglyoxal synthase

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Ribose utilization with an excess of mutarotase causes cell death due to accumulation of methylglyoxal

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Structural basis for the regulated protease and chaperone function of DegP

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Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain

21 January 2018

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The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K+ efflux system in Escherichia coli

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Characterization of the Escherichia coli YedU protein as a molecular chaperone

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Peptidase activity of the Escherichia coli Hsp31 chaperone

21 January 2018

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Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione

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Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli

21 January 2018

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Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions

21 January 2018

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The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad

21 January 2018

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21 January 2018

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Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures.

21 January 2018

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The linker-loop region of Escherichia coli chaperone Hsp31 functions as a gate that modulates high-affinity substrate binding at elevated temperatures

21 January 2018

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21 January 2018

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The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life

21 January 2018

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Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification--a role in pathogenesis and antiproliferative chemotherapy.

21 January 2018

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Glyoxalase I--structure, function and a critical role in the enzymatic defence against glycation

21 January 2018

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21 January 2018

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The 1.1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease

21 January 2018

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21 January 2018

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The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites

21 January 2018

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21 January 2018

Identifiers

DOI

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31 July 2017

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