Separation and evaluation of the covalent and noncovalent interactions which contribute to the binding of pyridoxal 5'-phosphate to D-serine apodehydratase.-Reference-Cited by-同舟云学术

Separation and evaluation of the covalent and noncovalent interactions which contribute to the binding of pyridoxal 5'-phosphate to D-serine apodehydratase.

Published:1975-07 Issue:14 Volume:250 Page:5359-5363
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Schonbeck N D,Skalski M,Shafer J A

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference11 articles.

1. STUDIES ON THE COENZYME ACTIVATION OF GLUTAMIC-ASPARTIC APOTRANSAMINASE

2. Analogs of Pyridoxal or Pyridoxal Phosphate: Relation of Structure to Binding with Apoenzymes and to Catalytic Activity

3. d-Serine Dehydratase from Escherichia coli

4. Coenzymatic Activity of Pyridoxal 5'-Sulfate and Related Analogues of Pyridoxal 5'-Phosphate

5. Resolution of D-serine dehydratase by cysteine. An analytical treatment.

Cited by 12 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Schiff bases formed between pyridoxal 5′-phosphate and Amino-β-cyclodextrins: Intramolecular remote ion pair interactions of the phosphate with ammonium moieties;Supramolecular Chemistry;1994-12

2. Disruption of active site interactions with pyridoxal 5'-phosphate and substrates by conservative replacements in the glycine-rich loop of Escherichia coli D-serine dehydratase;Journal of Biological Chemistry;1990-11

3. Contribution of a conserved arginine near the active site of Escherichia coli D-serine dehydratase to cofactor affinity and catalytic activity;Journal of Biological Chemistry;1989-02

4. The glycine-rich region of Escherichia coli D-serine dehydratase. Altered interactions with pyridoxal 5′-phosphate produced by substitution of aspartic acid for glycine.;Journal of Biological Chemistry;1988-11

5. D-serine dehydratase from Escherichia coli. DNA sequence and identification of catalytically inactive glycine to aspartic acid variants.;Journal of Biological Chemistry;1988-11