The excreted β-cyclopiazonate oxidocyclase isoenzymes from Penicillium cyclopium—III. Evidence for a ping-pong BI-BI mechanism from substrate inhibition studies-Reference-Cited by-同舟云学术

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The excreted β-cyclopiazonate oxidocyclase isoenzymes from Penicillium cyclopium—III. Evidence for a ping-pong BI-BI mechanism from substrate inhibition studies

Published:1979-01 Issue:1 Volume:10 Page:61-65
ISSN:0020-711X
Container-title:International Journal of Biochemistry
language:en
Short-container-title:International Journal of Biochemistry

Author:

Schabort J.C.,Marx M.

Publisher

Elsevier BV

Subject

Biochemistry

Reference14 articles.

1. Steady state kinetics;Cleland,1970

2. A reaction mechanism from steady state kinetic studies for O-acetylserine sulphhydrylase from Salmonella typhimurium LT2;Cook;J. biol. Chem.,1976

3. Steady state kinetics of high molecular weight (Type-1) NADH-dehydrogenase;Dooijewaard;Biochim. biophys. Acta,1976

4. Studies on the terminal electron transport system. I Succinic dehydrogenase;Green;J. biol. Chem.,1955

Cited by 4 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. Accessibility of the tryptophan residues and flavin prosthetic group of β-cyclopiazonate oxidocyclase to solvent studied by fluorescence quenching;International Journal of Biochemistry;1988-01

2. Oxidoreductases;Covalent Catalysis by Enzymes;1982

3. Biosynthesis of α-cyclopiazonic acid. Steric course of proton removal during the cyclisation of β-cyclopiazonic acid in Penicillium griseofulvum;J. Chem. Soc., Perkin Trans. 1;1981

4. β-Cyclopiazonate dehydrogenase;Springer Handbook of Enzymes

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