Metabolism of 2-ketoaldehydes in mold: purification and characterization of glyoxalase I from Aspergillus niger.

Metabolism of 2-ketoaldehydes in mold: purification and characterization of glyoxalase I from Aspergillus niger. Research Abstract Details 

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Metabolism of 2-ketoaldehydes in mold: purification and characterization of glyoxalase I from Aspergillus niger. Abstract Text:

Y Inoue,H Rhee,K Watanabe,K Murata,A Kimura,

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.

Metabolism of 2-ketoaldehydes in mold: purification and characterization of glyoxalase I from Aspergillus niger. Publishing Authors By Initials

Y Inoue,H Rhee,K Watanabe,K Murata,A Kimura,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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Metabolism of 2-ketoaldehydes in mold: purification and characterization of glyoxalase I from Aspergillus niger. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 102

Page Numbers: 583-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Sep

YEAR: 1987

Metabolism of 2-ketoaldehydes in mold: purification and characterization of glyoxalase I from Aspergillus niger. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Metabolism of 2-ketoaldehydes in mold: purification and characterization of glyoxalase I from Aspergillus niger. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: metabolism

Chemical & Substance for Abstract: Metabolism of 2-ketoaldehydes in mold: purification and characterization of glyoxalase I from Aspergillus niger. Information

Substance Name: Lactoylglutathione Lyase

Registry Number: EC 4.4.1.5

Grant and Affiliation Information for Metabolism of 2-ketoaldehydes in mold: purification and characterization of glyoxalase I from Aspergillus niger.

AFFILIATION: Research Institute for Food Science, Kyoto University.

Country: JAPAN

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MEDLINETA: J Biochem

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