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PMID: 7014916 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Limited proteolysis of N-(5'-phosphoribosyl)anthranilate isomerase: indoleglycerol phosphate synthase from Escherichia coli yields two different enzymically active, functional domains.

Journal of molecular biology ·Vol. 143 ·No. 4 ·1980-11-15 ·Pages 395-409

Kirschner K, Szadkowski H, Henschen A, Lottspeich F

Abstract

暂无摘要

MeSH Terms

Aldose-Ketose Isomerases Amino Acid Sequence Carbohydrate Epimerases/metabolism Carboxy-Lyases/metabolism Escherichia coli/enzymology Indole-3-Glycerol-Phosphate Synthase/metabolism Molecular Weight Peptide Fragments/isolation & purification Peptide Hydrolases

Chemicals

Peptide Fragments Peptide Hydrolases Carboxy-Lyases Indole-3-Glycerol-Phosphate Synthase Carbohydrate Epimerases Aldose-Ketose Isomerases phosphoribosylanthranilate isomerase

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Kirschner K

Szadkowski H

Henschen A

Lottspeich F

Article Info

Journal

Journal of molecular biology

Abbr.

J Mol Biol

ISSN

0022-2836

DOI

10.1016/0022-2836(80)90219-3

Published

1980-11-15

Pages

395-409

Language

English

Region

England

NLM ID

2985088R

Subset

External Links

PubMed source DOI: 10.1016/0022-2836(80)90219-3 View journal details

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Limited proteolysis of N-(5'-phosphoribosyl)anthranilate isomerase: indoleglycerol phosphate synthase from Escherichia coli yields two different enzymically active, functional domains.

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