Evidence for a Functional Glyoxylate Cycle in the Leishmaniae

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 1978 Sep 1

PMID 690079

Citations 7

Authors

M W Simon

E Martin

A J Mukkada

Affiliations

Soon will be listed here.

Abstract

Isocitrate lyase (EC 4.1.3.1) and malate synthase (EC 4.1.3.2), the two enzymes characteristic of the glyoxylate cycle, were demonstrated in promastigotes of five species of Leishmania (L. brasiliensis, L. donovani, L. mexicana, L. tarentolae, and L. tropica). Both enzymes were present in cells grown in a medium containing 10 mM glucose. Substitution of glucose with 20 mM acetate did not enhance enzyme levels. Acetate was readily taken up and metabolized by the cells. The distribution of label from acetate into various intermediary metabolites indicates a functional glyoxylate cycle and its role in gluconeogenesis/glyconeogenesis. The glyoxylate cycle in conjunction with alanine-glyoxylate aminotransferase and glyoxylate-aspartate aminotransferase could also be important in providing glyoxylate, the precursor for glycine biosynthesis.

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