Intracellular predominance of the pyridoxal 5′-phosphate form of aspartate aminotransferase in Escherichia coli B and reversible transformation of this form by extracellular substances-Reference-Cited by-同舟云学术

Intracellular predominance of the pyridoxal 5′-phosphate form of aspartate aminotransferase in Escherichia coli B and reversible transformation of this form by extracellular substances

Published:1989-04 Issue:4 Volume:71 Page:427-438
ISSN:0300-9084
Container-title:Biochimie
language:en
Short-container-title:Biochimie

Author:

Yagi Toshiharu,Niu Shigemitsu,Okawa Keiko,Yamamoto Sinpei,Nozaki Mitsuhiro

Publisher

Elsevier BV

Subject

General Medicine,Biochemistry

Reference20 articles.

1. Transaminases;Li,1985

2. Developmental profiles and properties of hepatic peroxisomal apo- and mitochondrial holoalanine:glyoxylate aminotransferase during chick embryogenesis.

3. Depletion of cultured human fibroblasts of pyridoxal 5′-phospate: Effect on activities of aspartate aminotransferase, alanine aminotransferase, and cystathionine β-synthase

4. Effect of vitamin B6 on the synthesis and degradation of aspartate aminotransferase in chicken embryo fibroblasts.

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1. Interaction of Pyridoxal 5′-Phosphate Form of Aspartate Aminotransferase with Vitamin B-6 Compounds and Antagonists in Rabbit Erythrocytes;Bioscience, Biotechnology, and Biochemistry;1993-01

2. Activity and spectroscopic properties of the Escherichia coli glutamate 1-semialdehyde aminotransferase and the putative active site mutant K265R;Biochemistry;1992-08-11

3. Hemolysate activation coefficient and its relationship to holoenzyme levels of aspartate aminotransefrase in rabbit erythrocytes;Nutrition Research;1991-04

4. Effect of Extracellularly Added Vitamin B-6 Compounds and Antagonists on Intracellular Pyridoxal 5’-Phosphate Form of Aspartate Aminotransferase in Rabbit Erythrocytes;Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors;1991