Structure-Based Mechanism for Early PLP-Mediated Steps of Rabbit Cytosolic Serine Hydroxymethyltrans...
Structure-Based Mechanism for Early PLP-Mediated Steps of Rabbit Cytosolic Serine Hydroxymethyltransferase Reaction
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Publisher
Cairo, Egypt: Hindawi Publishing Corporation
Journal title
Language
English
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Publisher
Cairo, Egypt: Hindawi Publishing Corporation
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Scope and Contents
Contents
Serine hydroxymethyltransferase catalyzes the reversible interconversion of L-serine and glycine with transfer of one-carbon groups to and from tetrahydrofolate. Active site residue Thr254 is known to be involved in the transaldimination reaction, a crucial step in the catalytic mechanism of all pyridoxal 5′-phosphate- (PLP-) dependent enzymes, whi...
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Full title
Structure-Based Mechanism for Early PLP-Mediated Steps of Rabbit Cytosolic Serine Hydroxymethyltransferase Reaction
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3728543
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3728543
Other Identifiers
ISSN
2314-6133
E-ISSN
2314-6141
DOI
10.1155/2013/458571
