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4 Multienzyme Complexes

1970
Publisher Summary This chapter discusses certain features of a few well-documented examples of multienzyme complexes. The multienzyme complexes that have been most thoroughly described are composed of two to six functionally related enzymes and have molecular weights ranging from a few hundred thousand to a few million. The particles contain definite
David J. Cox, Lester J. Reed
openaire   +2 more sources

Identification of two penicillin-binding multienzyme complexes in Haemophilus influenzae.

Biochemical and Biophysical Research Communications - BBRC, 1999
Dansyl-labeled penicillin, reversed-phase chromatography, and peptide mapping have been used to detect, separate, and study penicillin-binding proteins (PBPs) and PBP multienzyme complexes of H. influenzae.
Armin Alaedini, Richard A. Day
semanticscholar   +1 more source

Facilitation of Enzyme Catalysis by Formation of Multienzyme Complexes

1982
There has been considerable discussion whether enzymes, generally identified as constituent of ‘soluble cellular fraction’, may be organized into multienzyme complexes.1,2 Much attention has been paid to the possibility of complex formation between enzymes which catalyze successive reactions in the same metabolic pathway3-6.
SALERNO, Costantino, P. Fasella
openaire   +4 more sources

Multienzyme assembly of a p53 transcription complex

Nature Structural & Molecular Biology, 2007
Proline isomerization of the p53 transactivation domain has a central role in coordinating kinase signaling pathways that assemble the core p53 transcription complex.
Ted R. Hupp, Malcolm D. Walkinshaw
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D,L-S-methyllipoic acid methyl ester, a kinetically viable model for S-protonated lipoic acid as the oxidizing agent in reductive acyl transfers catalyzed by the 2-oxoacid dehydrogenase multienzyme complexes.

Biochemistry, 1998
D,L-S(6,8)-Methyllipoic acid methyl ester triflate salt (D,L-S-methyllipoic acid methyl ester) was synthesized as a model for S-protonated lipoic acid, suggested to be the active form of lipoic acid in the reductive acylation catalyzed by the E1 and E2 ...
K. Pan, F. Jordan
semanticscholar   +1 more source

Tryptophan synthase: A multienzyme complex with an intramolecular tunnel

The Chemical Record, 2001
AbstractTryptophan synthase is a classic enzyme that channels a metabolic intermediate, indole. The crystal structure of the tryptophan synthase α2β2 complex from Salmonella typhimurium revealed for the first time the architecture of a multienzyme complex and the presence of an intramolecular tunnel. This remarkable hydrophobic tunnel provides a likely
openaire   +3 more sources

Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase multienzyme complexes.

Biochemistry, 1989
Lipoamide and a peptide, Thr-Val-Glu-Gly-Asp-Lys-Ala-Ser-Met-Glu lipoylated on the N6-amino group of the lysine residue, were tested as substrates for reductive acetylation by the pyruvate decarboxylase (E1p) component of the pyruvate dehydrogenase ...
Lloyd D. Graham, L. Packman, R. Perham
semanticscholar   +1 more source

Affinity chromatography as a means to study multienzyme complexes involved in murein synthesis.

Microbial Drug Resistance, 1996
The interaction of murein hydrolases and synthases was studied by affinity chromatography. The lytic transglycosylases Slt70 and MltB of E. coli were purified and covalently linked to CNBr-activated Sepharose. Membrane extracts were analyzed for proteins
Moritz von Rechenberg   +2 more
semanticscholar   +1 more source

The role of multienzyme complexes in integration of cellular metabolism

Journal of Theoretical Biology, 1986
The notion of the "primary block" of cellular metabolism designated as "metabolic system" is introduced. Metabolic system is defined as a metabolic pathway which corresponds to the structurally ordered multienzyme complex. The complex of glycolytic enzymes which catalyzes the anaerobic reduction of glucose-6-phosphate with production of ATP may serve ...
openaire   +3 more sources

Reaction mechanism of the heterotetrameric (alpha2beta2) E1 component of 2-oxo acid dehydrogenase multienzyme complexes.

Biochemistry, 2003
Pyruvate decarboxylase (E1) catalyzes the first two reactions of the four involved in oxidative decarboxylation of pyruvate by the pyruvate dehydrogenase (PDH) multienzyme complex.
M. Fries, Hyo-Il Jung, R. Perham
semanticscholar   +1 more source

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