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Regulation of iso propyl malate isomerase ec 4.2.1.33 synthesis in neurospora crassa


, : Regulation of iso propyl malate isomerase ec 4.2.1.33 synthesis in neurospora crassa. Journal of Bacteriology 133(2): 794-801

The capacity to synthesize isopropylmalate isomerase (EC 4.2.1.33) by N. crassa increased during induction in the presence of cycloheximide but was inhibited by proflavine and other inhibitors of RNA synthesis. Turnover of the enzyme once formed appeared negligible, but the message (measured as enzyme-forming capacity) had a half-life of 4-8 min. A comparison of the kinetics of induction in the wild type and a newly isolated .alpha.-isopropylmalate-permeable strain suggested strongly that feedback control by leucine of .alpha.-isopropylmalate production can adequately serve as the primary physiological regulator of endogenous inducer concentration. Genetic data are presented which implicate the involvement of 2 unlinked genes, ipm-1 and imp-2, in determining permeation of .alpha.-isopropylmalate.

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Related references

Reichenbecher V.E.Jr; Gross S.R., 1974: Separation of transcription and translation of iso propyl malate isomerase messenger in neurospora crassa. Federation Proceedings 33(5 PART 2): 1464

Gross S.R., 1971: Iso propyl malate isomerase neurospora. Tabor, Herbert And Celia White Tabor (Edited By) Methods in Enzymology, Vol Xvii Metabolism Of Amino Acids And Amines Xxxi+1098p Illus Aca Demic Press: New York, N Y , U S A ; London, England 786-790

Reichenbecher, V.E.; Fischer, M.; Gross, S.R., 1978: Regulation of isopropylmalate isomerase synthesis in Neurospora crassa. The capacity to synthetize isopropylmalate isomerase (EC 4.2.1.33) by Neurospora crassa increased during induction in the presence of cycloheximide but was inhibited by proflavine and other inhibitors of RNA synthesis. Turnover of the enzyme once...

Stayanarayana, T.; Umbarger, H.E.; Lindegren, G., 1968: Biosynthesis of branched chain amino acids in yeast correlation of biochemical blocks and genetic lesions in leucine auxotrophs saccharomyces sp enz alpha iso propyl malate synthetase enz alpha iso propyl malate isomerase enz beta iso propyl malate dehydrogenase. Journal of Bacteriology 96(6): 2012-2017

Reichenbecher, V.E.J. ; Gross, S.R., 1978: Structural features of normal and complemented forms of the neurospora iso propyl malate isomerase ec 4.2.1.33. The isopropylmalate isomerase (EC 4.2.1.33) of N. crassa is a globular protein consisting of a single polypeptide chain with a MW of about 90,000. The isomerase cannot easily be freed of a contaminating protease which cleaves the enzyme into 2 maj...

Cho Chung Y.S.; Umbarger H.E., 1971: Iso propyl malate isomerase yeast. Tabor, Herbert And Celia White Tabor (Edited By) Methods in Enzymology, Vol Xvii Metabolism Of Amino Acids And Amines Xxxi+1098p Illus Aca Demic Press: New York, N Y , U S A ; London, England 782-785

Daivd, Rh, 1985: Regulation of polyamine synthesis in Neurospora crassa. UCLA symposia on molecular and cellular biology4(34): 145-146

Turner, J.R., 1968: Regulation of enzyme synthesis in Neurospora crassa. BNWL-714. Bnwl Reports . U.S. Atomic Energy Commission: 7.10-7.7+

Turner, J.R.; Matchett, W.H., 1966: Regulation of enzyme synthesis in Neurospora crassa. BNWL-480. Bnwl Reports . U.S. Atomic Energy Commission: 121-124

Sturani, E.; Costantini, M.G.; Zippel, R.; Alberghina, F.A., 1976: Regulation of RNA synthesis in Neurospora crassa. An analysis of a shift-up. A shift-up transition of growth from acetate to glucose is analyzed in Neurospora crassa. The rates of DNA and of protein accumulations remain at the preshift values for about 2 h, afterwards they increase to the rate characteristic of the new med...