ArticleThe Biochemical journal2007
The mechanism of addition of pyridoxal 5'-phosphate to Escherichia coli apo-serine hydroxymethyltransferase.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Impact of Ser81 phosphorylation on alanine: glyoxylate aminotransferase associated with Primary hyperoxaluria type I.Molecular biomedicine · 2026Article
- Insight into the dimer dissociation process of the Chromobacterium violaceum (S)-selective amine transaminase.Scientific reports · 2019Article
- Allosteric feedback inhibition of pyridoxine 5'-phosphate oxidase fromThe Journal of biological chemistry · 2019Article
- Engineering a pyridoxal 5'-phosphate supply for cadaverine production by using Escherichia coli whole-cell biocatalysis.Scientific reports · 2015Article
- Structure-based mechanism for early PLP-mediated steps of rabbit cytosolic serine hydroxymethyltransferase reaction.BioMed research international · 2013Article
- Extremophilic SHMTs: from structure to biotechnology.BioMed research international · 2013Review
- Campylobacter jejuni pdxA affects flagellum-mediated motility to alter host colonization.PloS one · 2013Article
- Serine hydroxymethyltransferase from the cold adapted microorganism Psychromonas ingrahamii: a low temperature active enzyme with broad substrate specificity.International journal of molecular sciences · 2012Article
- Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Catalytic and ligand-binding characteristics of Plasmodium falciparum serine hydroxymethyltransferase.Molecular and biochemical parasitology · 2009Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Previous studies suggest that the addition of pyridoxal 5'-phosphate to apo-serine hydroxymethyltransferase from Escherichia coli is the last event in the enzyme's folding process. We propose a mechanism for this reaction based on quenched-flow, stopped-flow and rapid-scanning stopped-flow experiments. All experiments were performed with an excess of apo-enzyme over cofactor, since excess pyridoxal 5'-phosphate results in a second molecule of cofactor binding to Lys346, which is part of the tetrahydropteroylglutamate-binding site. The equilibrium between the aldehyde and hydrate forms of the cofactor affects the kinetics of addition to the active site. Direct evidence of the formation of an intermediate aldimine between the cofactor and the active-site lysine was obtained. The results have been interpreted according to a three-step mechanism in which: (i) both aldehyde and hydrate forms of the cofactor bind rapidly and non-covalently to the apo-enzyme; (ii) only the aldehyde form reacts with the active-site lysine to give an intermediate internal aldimine with unusual spectral properties; and (iii) a final conformational change gives the native holo-enzyme.
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