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B6db references: 93205757

type Journal Article
authors Coccia, R.; Foppoli, C.; Blarzino, C.; De Marco, C.; Pensa, B.
title Transamination of some sulphur- or selenium-containing amino acids by bovine liver glutamine transaminase
journal Physiol Chem Phys Med NMR
ui 93205757
year (1992)
volume 24
number 4
pages 313-21
keywords Amino Acids/*metabolism
abstract S-(3-aminopropyl)cysteine and Se-(3-aminopropyl)selenocysteine are deaminated by bovine liver glutamine transaminase. The corresponding alpha-keto acids, S-(3-aminopropyl)-thiopyruvic acid and Se-(3- aminopropyl)selenopyruvic acid, are produced which spontaneously cyclize to ketimine derivatives. They have been identified by comparing their UV absorption spectra and some chemical or chromatographic properties with chemically synthesized authentic samples. Also S-(2- aminoethyl)homocysteine is the substrate for the enzyme. Kinetic parameters determined in comparison to thialysine and selenalysine show that neither the presence of a sulphur or a selenium atom nor the relative position of the atom in the carbon chain appreciably affects the substrate specificity of the enzyme. However, the length of the carbon chain has some influence on it.
last changed 2002/11/13 11:02

B6db references