| Literature DB >> 10641038 |
J B McNeil1, J Flynn, N Tsao, N Monschau, K Stahmann, R H Haynes, E M McIntosh, R E Pearlman.
Abstract
Genes encoding the mitochondrial (SHM1) and cytosolic (SHM2) serine hydroxymethyltransferases, and the L-threonine aldolase gene (GLY1) from Candida albicans were cloned and sequenced. All three genes are involved in glycine metabolism. The C. albicans Shm1 protein is 82% identical to that from Saccharomyces cerevisiae and 56% identical to that from Homo sapiens. The corresponding identities for the Shm2 proteins are 68% and 53%. The Gly1 protein shares significant identity with the S. cerevisiae L-threonine aldolase (55%) and also with threonine aldolases from Aeromonas jandiae (36%) and Escherichia coli (36%). Genetic ablation experiments show that GLY1 is a non-essential gene in C. albicans and that L-threonine aldolase plays a lesser role in glycine metabolism than it does in S. cerevisiae. GenBank Accession Nos of the C. albicans SHM1 and SHM2 are AF009965 and AF009966, respectively. Accession No. for C. albicans GLY1 is AF009967. Copyright 2000 John Wiley & Sons, Ltd.Entities:
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Year: 2000 PMID: 10641038 DOI: 10.1002/(SICI)1097-0061(20000130)16:2<167::AID-YEA519>3.0.CO;2-1
Source DB: PubMed Journal: Yeast ISSN: 0749-503X Impact factor: 3.239