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 |
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Hauptverfasser: | , |
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. |
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ISSN: | 0006-3002 1878-2434 |
DOI: | 10.1016/0006-3002(61)90513-3 |