DC Field | Value | Language |
---|---|---|
dc.contributor.author | Subedi, Krishna P. | ko |
dc.contributor.author | Choi, Dong-Wook | ko |
dc.contributor.author | Kim, In-Sook | ko |
dc.contributor.author | Min, Bum-Chan | ko |
dc.contributor.author | Park, Chan-Kyu | ko |
dc.date.accessioned | 2013-03-12T05:43:49Z | - |
dc.date.available | 2013-03-12T05:43:49Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2011-08 | - |
dc.identifier.citation | MOLECULAR MICROBIOLOGY, v.81, no.4, pp.926 - 936 | - |
dc.identifier.issn | 0950-382X | - |
dc.identifier.uri | http://hdl.handle.net/10203/101461 | - |
dc.description.abstract | Hsp31 encoded by hchA is known as a heat-inducible molecular chaperone. Although structure studies revealed that Hsp31 has a putative catalytic triad consisting of Asp-214, His-186 and Cys-185, its enzymatic function, besides weak amino-peptidase activity, is still unknown. We found that Hsp31 displays glyoxalase activity that catalyses the conversion of methylglyoxal (MG) to D-lactate without an additional cofactor. The glyoxalase activity was completely abolished in the hchA-deficient strain, confirming the relationship between the hchA gene and its enzymatic activity in vivo. Hsp31 exhibits Michaelis-Menten kinetics for substrates MG with K(m) and k(cat) of 1.43 +/- 0.12 mM and 156.9 +/- 5.5 min(-1) respectively. The highest glyoxalase activity was found at 35-40 degrees C and pH of 6.0-8.0, and the activity was significantly inhibited by Cu(2+), Fe(3+) and Zn(2+). Mutagenesis studies based on our evaluation of conserved catalytic residues revealed that the Cys-185 and Glu-77 were essential for catalysis, whereas His-186 was less crucial for enzymatic function, although it participates in the catalytic process. The stationary-phase Escherichia coli cells became more susceptible to MG when hchA was deleted, which was complemented by an expression of plasmid-encoded hchA. Furthermore, an accumulation of intracellular MG was observed in hchA-deficient strains. | - |
dc.language | English | - |
dc.publisher | WILEY-BLACKWELL | - |
dc.subject | MOLECULAR CHAPERONE | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | METHYLGLYOXAL | - |
dc.subject | PROTEIN | - |
dc.subject | SYSTEM | - |
dc.subject | DJ-1 | - |
dc.subject | GENE | - |
dc.subject | DETOXIFICATION | - |
dc.subject | TEMPERATURES | - |
dc.subject | GLUTATHIONE | - |
dc.title | Hsp31 of Escherichia coli K-12 is glyoxalase III | - |
dc.type | Article | - |
dc.identifier.wosid | 000293752500007 | - |
dc.identifier.scopusid | 2-s2.0-80051560164 | - |
dc.type.rims | ART | - |
dc.citation.volume | 81 | - |
dc.citation.issue | 4 | - |
dc.citation.beginningpage | 926 | - |
dc.citation.endingpage | 936 | - |
dc.citation.publicationname | MOLECULAR MICROBIOLOGY | - |
dc.contributor.localauthor | Park, Chan-Kyu | - |
dc.contributor.nonIdAuthor | Kim, In-Sook | - |
dc.contributor.nonIdAuthor | Min, Bum-Chan | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | MOLECULAR CHAPERONE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | METHYLGLYOXAL | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | SYSTEM | - |
dc.subject.keywordPlus | DJ-1 | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | DETOXIFICATION | - |
dc.subject.keywordPlus | TEMPERATURES | - |
dc.subject.keywordPlus | GLUTATHIONE | - |
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