METABOLISM OF L-LYSINE BY BACTERIAL ENZYMES:IV. δ-AMINOVALERIC ACID-GLUTAMIC ACID TRANSAMINASE
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- ICHIHARA AKIRA
- Department of Physiological Chemistry, Medical School, Institute for Protein Research, Osaka University
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- ICHIHARA ELIZABETH A.
- Department of Physiological Chemistry, Medical School, Institute for Protein Research, Osaka University
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- SUDA MASAMI
- Department of Physiological Chemistry, Medical School, Institute for Protein Research, Osaka University
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説明
1. δ-Aminovaleric acid-glutamic acid transaminase was isolated from Pseudomonas and purified.<br> 2. This enzyme catalyzes the following reaction:<br> δ-aminovaleric acid+α-ketoglutaric acid_??_glutaric semialdehyde+L-glutamic acid<br> Substrate specificity was restricted to α-aminovaleric acid and α-ketoglutaric acid. None of the several amino acids nor pyruvic acid tested were inactive. Glutaric semialdehyde was identified as the product of the forward reaction and δ-aminovaleric acid as that of the reverse reaction.<br> The authors wish to thank Drs. S. Akabori and T. Okuda of this Institute for generous supply of glutaric semialdehyde ethylester.
収録刊行物
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- The Journal of Biochemistry
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The Journal of Biochemistry 48 (3), 412-420, 1960
The Japanese Biochemical Society
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詳細情報 詳細情報について
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- CRID
- 1573387452940379264
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- NII論文ID
- 130003536573
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- ISSN
- 0021924X
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- 本文言語コード
- en
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- データソース種別
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- CiNii Articles