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Serine hydroxymethyltransferase and threonine aldolase: are they identical?
Int J Biochem Cell Biol. 2000 Mar; 32(3):289-301.IJ

Abstract

Serine hydroxymethyltransferase, a pyridoxal phosphate-dependent enzyme, catalyses the interconversion of serine and glycine, both of which are major sources of one-carbon units necessary for the synthesis of purine, thymidylate, methionine, and so on. Threonine aldolase catalyzes the pyridoxal phosphate-dependent, reversible reaction between threonine and acetaldehyde plus glycine. No extensive studies have been carried out on threonine aldolase in animal tissues, and it has long been believed that serine hydroxymethyltransferase and threonine aldolase are the same, i.e. one entity. This is based on the finding that rabbit liver serine hydroxymethyltransferase possesses some threonine aldolase activity. Recently, however, many kinds of threonine aldolase and corresponding genes were isolated from micro-organisms, and these enzymes were shown to be distinct from serine hydroxymethyltransferase. The experiments with isolated hepatocytes and cell-free extracts from various animals revealed that threonine is degraded mainly through the pathway initiated by threonine 3-dehydrogenase, and there is little or no contribution by threonine aldolase. Thus, although serine hydroxymethyltransferase from some mammalian livers exhibits a low threonine aldolase activity, the two enzymes are distinct from each other and mammals lack the "genuine" threonine aldolase.

Authors+Show Affiliations

Department of Biochemistry, Faculty of Medicine, Toyama Medical and Pharmaceutical University, Japan. hogawa@ms.toyama-mpu.ac.jpNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Review

Language

eng

PubMed ID

10716626

Citation

Ogawa, H, et al. "Serine Hydroxymethyltransferase and Threonine Aldolase: Are They Identical?" The International Journal of Biochemistry & Cell Biology, vol. 32, no. 3, 2000, pp. 289-301.
Ogawa H, Gomi T, Fujioka M. Serine hydroxymethyltransferase and threonine aldolase: are they identical? Int J Biochem Cell Biol. 2000;32(3):289-301.
Ogawa, H., Gomi, T., & Fujioka, M. (2000). Serine hydroxymethyltransferase and threonine aldolase: are they identical? The International Journal of Biochemistry & Cell Biology, 32(3), 289-301.
Ogawa H, Gomi T, Fujioka M. Serine Hydroxymethyltransferase and Threonine Aldolase: Are They Identical. Int J Biochem Cell Biol. 2000;32(3):289-301. PubMed PMID: 10716626.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Serine hydroxymethyltransferase and threonine aldolase: are they identical? AU - Ogawa,H, AU - Gomi,T, AU - Fujioka,M, PY - 2000/3/15/pubmed PY - 2000/4/29/medline PY - 2000/3/15/entrez SP - 289 EP - 301 JF - The international journal of biochemistry & cell biology JO - Int J Biochem Cell Biol VL - 32 IS - 3 N2 - Serine hydroxymethyltransferase, a pyridoxal phosphate-dependent enzyme, catalyses the interconversion of serine and glycine, both of which are major sources of one-carbon units necessary for the synthesis of purine, thymidylate, methionine, and so on. Threonine aldolase catalyzes the pyridoxal phosphate-dependent, reversible reaction between threonine and acetaldehyde plus glycine. No extensive studies have been carried out on threonine aldolase in animal tissues, and it has long been believed that serine hydroxymethyltransferase and threonine aldolase are the same, i.e. one entity. This is based on the finding that rabbit liver serine hydroxymethyltransferase possesses some threonine aldolase activity. Recently, however, many kinds of threonine aldolase and corresponding genes were isolated from micro-organisms, and these enzymes were shown to be distinct from serine hydroxymethyltransferase. The experiments with isolated hepatocytes and cell-free extracts from various animals revealed that threonine is degraded mainly through the pathway initiated by threonine 3-dehydrogenase, and there is little or no contribution by threonine aldolase. Thus, although serine hydroxymethyltransferase from some mammalian livers exhibits a low threonine aldolase activity, the two enzymes are distinct from each other and mammals lack the "genuine" threonine aldolase. SN - 1357-2725 UR - https://www.unboundmedicine.com/medline/citation/10716626/Serine_hydroxymethyltransferase_and_threonine_aldolase:_are_they_identical DB - PRIME DP - Unbound Medicine ER -