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Serine hydroxymethyltransferase: a model enzyme for mechanistic, structural, and evolutionary studies.
Biochim Biophys Acta. 2011 Nov; 1814(11):1489-96.BB

Abstract

Serine hydroxymethyltransferase is a ubiquitous representative of the family of fold type I, pyridoxal 5'-phosphate-dependent enzymes. The reaction catalyzed by this enzyme, the reversible transfer of the Cβ of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes. Serine hydroxymethyltransferase has been intensively investigated because of the interest aroused by the complex mechanism of the hydroxymethyltransferase reaction and its broad substrate and reaction specificity. Although the increasing availability of crystallographic data and the characterization of several site-specific mutants helped in understanding previous functional and structural studies, they also represent the starting point of novel investigations. This review will focus on recently highlighted catalytic, structural, and evolutionary aspects of serine hydroxymethyltransferase. This article is part of a Special Issue entitled: Pyridoxal phosphate Enzymology.

Authors+Show Affiliations

Departimento di Scienze Biochimiche A. Rossi Fanelli and Instituto Pasteur- Fondazione Cenci Bolognetti, Sapienza Università di Roma, Piazzale Aldo Moro 5, 00185 Roma, Italy.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Review

Language

eng

PubMed ID

21059411

Citation

Florio, Rita, et al. "Serine Hydroxymethyltransferase: a Model Enzyme for Mechanistic, Structural, and Evolutionary Studies." Biochimica Et Biophysica Acta, vol. 1814, no. 11, 2011, pp. 1489-96.
Florio R, di Salvo ML, Vivoli M, et al. Serine hydroxymethyltransferase: a model enzyme for mechanistic, structural, and evolutionary studies. Biochim Biophys Acta. 2011;1814(11):1489-96.
Florio, R., di Salvo, M. L., Vivoli, M., & Contestabile, R. (2011). Serine hydroxymethyltransferase: a model enzyme for mechanistic, structural, and evolutionary studies. Biochimica Et Biophysica Acta, 1814(11), 1489-96. https://doi.org/10.1016/j.bbapap.2010.10.010
Florio R, et al. Serine Hydroxymethyltransferase: a Model Enzyme for Mechanistic, Structural, and Evolutionary Studies. Biochim Biophys Acta. 2011;1814(11):1489-96. PubMed PMID: 21059411.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Serine hydroxymethyltransferase: a model enzyme for mechanistic, structural, and evolutionary studies. AU - Florio,Rita, AU - di Salvo,Martino Luigi, AU - Vivoli,Mirella, AU - Contestabile,Roberto, Y1 - 2010/11/05/ PY - 2010/09/24/received PY - 2010/10/25/revised PY - 2010/10/29/accepted PY - 2010/11/10/entrez PY - 2010/11/10/pubmed PY - 2011/12/20/medline SP - 1489 EP - 96 JF - Biochimica et biophysica acta JO - Biochim Biophys Acta VL - 1814 IS - 11 N2 - Serine hydroxymethyltransferase is a ubiquitous representative of the family of fold type I, pyridoxal 5'-phosphate-dependent enzymes. The reaction catalyzed by this enzyme, the reversible transfer of the Cβ of serine to tetrahydropteroylglutamate, represents a link between amino acid and folates metabolism and operates as a major source of one-carbon units for several essential biosynthetic processes. Serine hydroxymethyltransferase has been intensively investigated because of the interest aroused by the complex mechanism of the hydroxymethyltransferase reaction and its broad substrate and reaction specificity. Although the increasing availability of crystallographic data and the characterization of several site-specific mutants helped in understanding previous functional and structural studies, they also represent the starting point of novel investigations. This review will focus on recently highlighted catalytic, structural, and evolutionary aspects of serine hydroxymethyltransferase. This article is part of a Special Issue entitled: Pyridoxal phosphate Enzymology. SN - 0006-3002 UR - https://www.unboundmedicine.com/medline/citation/21059411/Serine_hydroxymethyltransferase:_a_model_enzyme_for_mechanistic_structural_and_evolutionary_studies_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1570-9639(10)00284-0 DB - PRIME DP - Unbound Medicine ER -