The glycine-rich region of Escherichia coli D-serine dehydratase. Altered interactions with pyridoxal 5′-phosphate produced by substitution of aspartic acid for glycine.-Reference-Cited by-同舟云学术

The glycine-rich region of Escherichia coli D-serine dehydratase. Altered interactions with pyridoxal 5′-phosphate produced by substitution of aspartic acid for glycine.

Published:1988-11 Issue:32 Volume:263 Page:16934-16941
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Marceau M,Lewis S D,Shafer J A

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference48 articles.

1. D-serine dehydratase from Escherichia coli. DNA sequence and identification of catalytically inactive glycine to aspartic acid variants.

2. Crystallographic studies on the activity of glycogen phosphorylase b

3. Substrate-cofactor interactions for glycogen phosphorylase b: a binding study in the crystal with heptenitol and heptulose 2-phosphate

4. Pyridoxal phosphate site in glycogen phosphorylase b: structure in native enzyme and in three derivatives with modified cofactors

5. Two conformations of crystalline adenylate kinase

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