Purification of 7-Keto-8-aminopelargonic Acid-7, 8-Diaminopelargonic Acid Aminotransferase, an Enzyme Involved in Biotin Biosynthesis, from Brevibacterium divaricatum
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منابع مشابه
Purification and properties of 7, 8-diaminopelargonic acid aminotransferase.
The enzyme 7, 8-diaminopelargonic acid aminotransferase utilizes S-adenosyl-L-methionine to transaminate the biotin precurson 7-keto-8-aminopelargonic acid and form the next intermediate in the pathway, 7, 8-diaminopelargonic acid. The enzyme has been purified nearly 1000-fold from an extract of a regulatory mutant of Escherichia coli which is derepressed for the enzymes of the biotin operon. T...
متن کاملBiosynthesis of 7, 8-diaminopelargonic acid from 7-keto-8-aminopelargonic acid and S-adenosyl-L-methionine. The kinetics of the reaction.
The transamination of 7-keto-8-aminopelargonic acid by 7, 8-diaminopelargonic acid aminotransferase of Escherichia coli requires S-adenosyl-L-methionine as the amino donor. Initial velocity studies of this reaction revealed a parallel pattern of reciprocal plots characteristic of a ping-pong mechanism. m-Keto-8-aminopelargonic acid showed strong substrate inhibition which was competitive with S...
متن کاملBroad Substrate Stereospecificity of the Mycobacterium tuberculosis 7-Keto-8-aminopelargonic Acid Synthase
Biotin is an essential enzyme cofactor required for carboxylation and transcarboxylation reactions. The absence of the biotin biosynthesis pathway in humans suggests that it can be an attractive target for the development of novel drugs against a number of pathogens. 7-Keto-8-aminopelargonic acid (KAPA) synthase (EC 2.3.1.47), the enzyme catalyzing the first committed step in the biotin biosynt...
متن کاملBroad substrate stereospecificity of the Mycobacterium tuberculosis 7-keto-8-aminopelargonic acid synthase: Spectroscopic and kinetic studies.
Biotin is an essential enzyme cofactor required for carboxylation and transcarboxylation reactions. The absence of the biotin biosynthesis pathway in humans suggests that it can be an attractive target for the development of novel drugs against a number of pathogens. 7-Keto-8-aminopelargonic acid (KAPA) synthase (EC 2.3.1.47), the enzyme catalyzing the first committed step in the biotin biosynt...
متن کاملBiotin synthesis in plants. The first committed step of the pathway is catalyzed by a cytosolic 7-keto-8-aminopelargonic acid synthase.
Biochemical and molecular characterization of the biotin biosynthetic pathway in plants has dealt primarily with biotin synthase. This enzyme catalyzing the last step of the pathway is localized in mitochondria. Other enzymes of the pathway are however largely unknown. In this study, a genomic-based approach allowed us to clone an Arabidopsis (Arabidopsis thaliana) cDNA coding 7-keto-8-aminopel...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1973
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.37.2683