The substrate specificity of l-alanine dehydrogenase

l-Alanine dehydrogenase complexes with l-alanine and several of its analogues. Glycine, sarcosine and structural analogues of alanine having alkyl, hydroxymethyl or thiomethyl substitutions on the α-carbon of alanine bind with the enzyme. The l-isomers of these amino acids are substrates while the d...

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Veröffentlicht in:Biochimica et biophysica acta 1961-03, Vol.48 (1), p.47-55
Hauptverfasser: O'Connor, R.J., Halvorson, H.
Format: Artikel
Sprache:eng
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Zusammenfassung:l-Alanine dehydrogenase complexes with l-alanine and several of its analogues. Glycine, sarcosine and structural analogues of alanine having alkyl, hydroxymethyl or thiomethyl substitutions on the α-carbon of alanine bind with the enzyme. The l-isomers of these amino acids are substrates while the d-isomers, glycine, and sarcosine are competitive inhibitors of l-alanine deamination. Substitution or modification of the -COOH group, the -NH 2 group or the -H of the α-carbon of l-alanine results in complete loss of complexing ability. As in the case of glutamic acid dehydrogenase, l-alanine dehydrogenase metabolizes aliphatic amino acids with chain lengths of less than 7 carbons and is inhibited by the d-isomers of its substrates.
ISSN:0006-3002
1878-2434
DOI:10.1016/0006-3002(61)90513-3