Document Detail

Metabolism of 2-ketoaldehydes in mold: purification and characterization of glyoxalase I from Aspergillus niger.
MedLine Citation:
PMID:  3123469     Owner:  NLM     Status:  MEDLINE    
Glyoxalase I catalyzing the conversion of methylglyoxal into S-lactoylglutathione in the presence of glutathione was purified approximately 1,400-fold with 2.9% activity yield from mold, Aspergillus niger. The enzyme consisted of a single polypeptide chain with a relative molecular weight of 36,000 on both SDS-polyacrylamide gel electrophoresis and Sephadex G-150 gel filtration. The enzyme was most active at pH 7.0, 35-37 degrees C. Among the various aldehydes tested, the enzyme was active on methylglyoxal and 4,5-dioxovalerate with Km values of 1.25 and 0.87 mM, respectively. The activity of the enzyme was completely inhibited by Zn2+ at 0.5 mM. An equimolar amount of EDTA (0.5 mM) protected the enzyme from inactivation by Zn2+. EDTA competitively (K1 = 1.3 mM) inhibited the activity of the enzyme. Fe2+ was a potent activator for the enzyme, the activation being approximately 2.4-fold at 0.5 mM.
Y Inoue; H Rhee; K Watanabe; K Murata; A Kimura
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of biochemistry     Volume:  102     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  1987 Sep 
Date Detail:
Created Date:  1988-03-07     Completed Date:  1988-03-07     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  583-9     Citation Subset:  IM    
Research Institute for Food Science, Kyoto University.
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MeSH Terms
Aldehydes / metabolism*
Aspergillus niger / enzymology*
Chromatography, DEAE-Cellulose
Edetic Acid / pharmacology
Electrophoresis, Polyacrylamide Gel
Lactoylglutathione Lyase / analysis,  isolation & purification,  metabolism*
Lyases / metabolism*
Molecular Weight
Pyruvaldehyde / metabolism*
Substrate Specificity
Reg. No./Substance:
0/Aldehydes; 60-00-4/Edetic Acid; 78-98-8/Pyruvaldehyde; EC 4.-/Lyases; EC Lyase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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