EC 2.4.1.48

EC 2.4.1.48

ENZYME entry: EC ExplorEnz, PRIAM enzyme-specific profiles, KEGG Ligand Database for Enzyme Nomenclature.
EC Number: . The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Accepted Name. Heteroglycan alpha-mannosyltransferase. Reaction catalysed. GDP-mannose + heteroglycan GDP + 2(or.

EC 2.4.1.48 - for mac

He is the author and editor of numerous scientific publications. Use of this online version of BRENDA is free for academic research only. View entry in raw text format no links. Mannosyl transfer in Cryptococcus laurentii. Kinetic mechanisms have played a major role in defining the metabolic pathways, the mechanistic action... EC 2.4.1.48
Please login to EC 2.4.1.48 access to the AMENDA and FRENDA data The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae. The acceptor is a heteroglycan primer containing mannose, galactose and xylose. Data sheets are arranged in their EC-Number sequence and the volumes themselves are EC 2.4.1.48 according to enzyme classes. The Handbook of Biochemical Kinetics provides the "underlying scaffolding" of logic for kinetic approaches to distinguish rival models or mechanisms. Mannosyl transfer in Cryptococcus laurentii. Springer Handbook of Enzymes provides data on enzymes sufficiently well characterized. Each entry is correlated with references and one or more source organisms.

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1251 AVENUE OF THE AMERICAS 21ST FLOOR Purich is currently a Professor and Chairman of the Department of Biochemistry and Molecular Biology at the Florida College of Medicine. View entry in raw text format no links. Back to the Top Heteroglycan alpha-mannosyltransferase. Mannosyl transfer in Cryptococcus EC 2.4.1.48. This new, second edition reflects considerable progress in enzymology: many enzymes are newly classified or reclassified.
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