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Kreft BD, Townsend A, Pohlenz HD, et al. Purification and Properties of Cystathionine [gamma]-Synthase from Wheat (Triticum aestivum L.). Plant Physiol. 1994;104(4):1215-1220doi: 10.1104/pp.104.4.1215.
Kreft, B. D., Townsend, A., Pohlenz, H. D., & Laber, B. (1994). Purification and Properties of Cystathionine [gamma]-Synthase from Wheat (Triticum aestivum L.). Plant physiology, 104(4), 1215-1220. https://doi.org/10.1104/pp.104.4.1215
Kreft, B. D., et al. "Purification and Properties of Cystathionine [gamma]-Synthase from Wheat (Triticum aestivum L.)." Plant physiology vol. 104,4 (1994): 1215-1220. doi: https://doi.org/10.1104/pp.104.4.1215
Kreft BD, Townsend A, Pohlenz HD, Laber B. Purification and Properties of Cystathionine [gamma]-Synthase from Wheat (Triticum aestivum L.). Plant Physiol. 1994 Apr;104(4):1215-1220. doi: 10.1104/pp.104.4.1215. PMID: 12232160; PMCID: PMC159283.
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Plant Physiol. 1994 Apr;104(4):1215-1220. doi: 10.1104/pp.104.4.1215.

Purification and Properties of Cystathionine [gamma]-Synthase from Wheat (Triticum aestivum L.).

Plant physiology

B. D. Kreft, A. Townsend, H. D. Pohlenz, B. Laber

Affiliations

  1. Schering AG, Agrochemical Research, D-13342 Berlin, Germany.

PMID: 12232160 PMCID: PMC159283 DOI: 10.1104/pp.104.4.1215

Abstract

Cysthathionine [gamma]-synthase (CS), an enzyme involved in methionine biosynthesis, was purified from an acetone powder prepared from wheat (Triticum aestivum L.). After several chromatographic steps and radiolabeling of the partially purified enzyme with sodium cyanoboro[3H]hydride, a single polypeptide with a molecular weight of 34,500 was isolated by sodium dodecyl sulfate-high performance electrophoresis chromatography. Since the molecular weight of the native enzyme was 155,000, CS apparently consists of four identical subunits. The pyridoxal 5[prime]-phosphate-dependent forward reaction has a pH optimum of 7.5 and follows a hybrid ping-pong mechanism with Km values of 3.6 mM and 0.5 mM for L-homoserine phosphate and L-cysteine, respectively. L-Cysteine methyl ester, thioglycolate methyl ester, and sodium sulfide were also utilized as thiol substrates. The latter observation suggests that CS and phosphohomoserine sulfhydrase might be a single enzyme. CS does not seem to be a regulatory enzyme but was irreversibly inhibited by DL-propargylglycine (Ki = 45 [mu]M, Kinact = 0.16 min-1). Furthermore, the homoserine phosphate analogs 4-(phosphonomethyl)-pyridine-2-carboxylic acid, Z-3-(2-phosphonoethen-1-yl)pyridine-2-carboxylic acid, and DL-E-2-amino-5-phosphono-3-pentenoic acid acted as reversible competitive inhibitors with Ki values of 45, 40, and 1.1 [mu]M, respectively.

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