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PMID: 14291582 Published · ppublish English Journal Article

INCREASED ACTIVITY OF TRYPTOPHAN BIOSYNTHETIC ENZYMES IN HISTIDINE MUTANTS OF NEUROSPORA CRASSA.

Journal of bacteriology ·Vol. 89 ·1965-06-00 ·Pages 1472-7

CARSIOTIS M, LACY AM

Abstract

Carsiotis, M. (University of Cincinnati College of Medicine, Cincinnati, Ohio), and Ann M. Lacy. Increased activity of tryptophan biosynthetic enzymes in histidine mutants of Neurospora crassa. J. Bacteriol. 89:1472-1477. 1965.-The activities of tryptophan synthetase and indoleglycerol phosphate synthetase, the last two enzymes in the tryptophan biosynthetic pathway, are elevated twofold or more in all histidine mutants of Neurospora crassa. The elevation occurs only when the mutants are grown in a histidine-limited medium. Several possible mechanisms for this elevation were disproved experimentally. The cause of the elevated enzyme activities remains unknown.

Keywords
AMINO ACID METABOLISM EXPERIMENTAL LAB STUDY GLYCEROPHOSPHATES HISTIDINE INDOLES LIGASES METABOLISM MUTATION NEUROSPORA PHARMACOLOGY PYROPHOSPHATASE SUCROSE TRYPTOPHAN
MeSH Terms
Amino Acids/metabolism Glycerophosphates Histidine Indoles Ligases Metabolism Mutation Neurospora Neurospora crassa Pharmacology Pyrophosphatases Research Sucrose Tryptophan
Chemicals
Amino Acids Glycerophosphates Indoles indoleglycerol phosphate Histidine Sucrose Tryptophan Pyrophosphatases Ligases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
CARSIOTIS M
LACY A M
References (22)
22 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.89.6.1472-1477.1965
Published
1965-06-00
Pages
1472-7
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC277678
Subset
OM
External Links
PubMed source DOI: 10.1128/jb.89.6.1472-1477.1965 PMC Full Text View journal details
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