Selenomethionine is as a good substrate as methionine for bovine liver glutamine transaminase (E.C. 2.6.1.15). Almost identical Km values for methionine, selenomethionine, 4-methylthio-2-oxobutanoic acid and 4-methylseleno-2-oxobutanoic acid have been obtained. Like for other enzymes, also for glutamine transaminase the substitution of the sulfur atom in a substrate molecule by a selenium one does not appreciably affect the enzyme affinity. Glutamine transaminase may thus be involved in selenomethionine catabolism.

Selenomethionine as substrate for glutamine transaminase / Blarzino, Carla; Coccia, Raffaella; B., Pensa; Cini, Chiara; C. D., Marco. - In: BIOCHEMISTRY AND MOLECULAR BIOLOGY INTERNATIONAL. - ISSN 1039-9712. - STAMPA. - 32:(1994), pp. 79-86.

Selenomethionine as substrate for glutamine transaminase.

BLARZINO, Carla;COCCIA, Raffaella;CINI, Chiara;
1994

Abstract

Selenomethionine is as a good substrate as methionine for bovine liver glutamine transaminase (E.C. 2.6.1.15). Almost identical Km values for methionine, selenomethionine, 4-methylthio-2-oxobutanoic acid and 4-methylseleno-2-oxobutanoic acid have been obtained. Like for other enzymes, also for glutamine transaminase the substitution of the sulfur atom in a substrate molecule by a selenium one does not appreciably affect the enzyme affinity. Glutamine transaminase may thus be involved in selenomethionine catabolism.
1994
Animals, Cattle, Chromatography; High Pressure Liquid, Kinetics, Liver; enzymology, Methionine; analogs /&/ derivatives/chemistry/metabolism, Selenomethionine; analogs /&/ derivatives/chemistry/metabolism, Substrate Specificity, Transaminases; metabolism
01 Pubblicazione su rivista::01a Articolo in rivista
Selenomethionine as substrate for glutamine transaminase / Blarzino, Carla; Coccia, Raffaella; B., Pensa; Cini, Chiara; C. D., Marco. - In: BIOCHEMISTRY AND MOLECULAR BIOLOGY INTERNATIONAL. - ISSN 1039-9712. - STAMPA. - 32:(1994), pp. 79-86.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/470023
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