Files and links (1)
Published, Version of Record (VoR)CC BY V4.0, Open
Journal article
Sequence Analysis of Sarcosine Oxidase and Nearby Genes Reveals Homologies with Key Enzymes of Folate One-carbon Metabolism
The Journal of biological chemistry, v 270(31), pp 18252-18259
04 Aug 1995
PMID: 7543100
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Corynebacterial sarcosine oxidase, a heterotetrameric (αβγδ) enzyme containing covalent and noncovalent FAD, catalyzes the oxidative demethylation of sarcosine to yield glycine, H2O2, and 5,10-CH2-tetrahydrofolate (H4 folate) in a reaction requiring H4folate and O2. The sarcosine oxidase operon contains at least five closely packed genes encoding sarcosine oxidase subunits and serine hydroxymethyltransferase (glyA), arranged in the order glyAsoxBDAG. The operon status of a putative purU gene, found 340 nucleotides downstream from soxG, is not known. No homology with other proteins is observed for the smallest sarcosine oxidase subunits γ and δ. The β subunit (405 residues) contains an ADP-binding motif near its NH2 terminus, the covalent FAD attachment site (H175), and exhibits homology with the NH2-terminal half of dimethylglycine dehydrogenase (857 residues) and monomeric, bacterial sarcosine oxidases (~388 residues), enzymes that contain a single covalent FAD. The α subunit (967 residues) contains a second ADP-binding motif within an ~280 residue region near the NH2 terminus that exhibits homology with subunit A from octopine and nopaline oxidases, heterodimeric enzymes that catalyze analogous oxidative cleavage reactions with N-substituted arginine derivatives. An ~380 residue region near the COOH terminus of α exhibits homology with T-protein and the COOH-terminal half of dimethylglycine dehydrogenase. These enzymes catalyze the formation of 5,10-CH2-H4folate, using different one-carbon donors. The results suggest that the α subunit and dimethylglycine dehydrogenase contain an NH2-terminal domain that binds noncovalent or covalent FAD, respectively, and a carboxyl-terminal H4folate-binding domain.
Metrics
Details
- Title
- Sequence Analysis of Sarcosine Oxidase and Nearby Genes Reveals Homologies with Key Enzymes of Folate One-carbon Metabolism
- Creators
- Lawrence J. Chlumsky - Hahnemann University HospitalLening Zhang - From the Department of Biological Chemistry, Hahnemann University School of Medicine, Philadelphia, Pennsylvania 19102Marilyn Schuman Jorns - From the Department of Biological Chemistry, Hahnemann University School of Medicine, Philadelphia, Pennsylvania 19102
- Publication Details
- The Journal of biological chemistry, v 270(31), pp 18252-18259
- Publisher
- Elsevier
- Grant note
- GM 31704 / National Institutes of Health
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:A1995RM64200018
- Scopus ID
- 2-s2.0-0029143934
- Other Identifier
- 991019183990504721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology