Mutation of Gly-444 inactivates the S. pombe malic enzyme
Date
1998
Authors
Viljoen M.
Van Der Merwe M.
Subden R.E.
Van Vuuren H.J.J.
Journal Title
Journal ISSN
Volume Title
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Abstract
A mutant malic enzyme gene, mae2-, was cloned from a strain of Schizosaccharomyces pombe that displayed almost no malic enzyme activity. Sequence analysis revealed only one codon-altering mutation, a guanine to adenine at nucleotide 1331, changing the glycine residue at position 444 to an aspartate residue. Gly-444 is located in Region H, previously identified as one of eight highly conserved regions in malic enzymes. We found that Gly-444 is absolutely conserved in 27 malic enzymes from various prokaryotic and eukaryotic sources, as well as in three bacterial malolactic enzymes investigated. The evolutionary conservation of Gly-444 suggests that this residue is important for enzymatic function. Copyright (C) 1998 Federation of European Microbiological Societies.
Description
Keywords
malate dehydrogenase (decarboxylating), malic acid, article, enzyme inactivation, eukaryote, mutation, nonhuman, nucleotide sequence, priority journal, schizosaccharomyces pombe, Amino Acid Sequence, Blotting, Northern, Blotting, Western, Cloning, Molecular, Conserved Sequence, DNA, Fungal, Genes, Fungal, Glycine, Malate Dehydrogenase, Malates, Molecular Sequence Data, Point Mutation, Polymerase Chain Reaction, Restriction Mapping, Schizosaccharomyces, Sequence Analysis, DNA, Structure-Activity Relationship, Bacteria (microorganisms), Eukaryota, Prokaryota, Schizosaccharomyces pombe
Citation
FEMS Microbiology Letters
167
2
167
2