Catalytic and spectroscopic characterisation of a copper-substituted alcohol dehydrogenase from yeast.
Yeast alcohol dehydrogenase (Y-ADH) is widely studied for its biotechnological importance and various attempts to improve its catalytic properties have been made. In this paper, a catalytically active metal-substituted Y-ADH was prepared in vitro by substituting one zinc atom with copper. EPR and Raman spectroscopy suggest that copper maintains the same co-ordination geometry as zinc in native Y-ADH. The active Cu-ADH shows lower substrate affinity and lower specific activity (SA) than native ADH, but greater than a previously obtained Co-ADH. Furthermore, Cu-ADH maintains its catalytic efficiency in a wider pH range than native enzyme.
Vanni
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Dipartimento di Chimica Analitica, Università di Torino, V. Giuria 5, 10125 Turin, Italy. vanni@ch.unito.it
Anfossi
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L
Pessione
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Giovannoli
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C
D000426:Alcohol Dehydrogenase / Q000737:chemistry* / Q000378:metabolism*; D002384:Catalysis; D003300:Copper / Q000737:chemistry; D004578:Electron Spin Resonance Spectroscopy; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013059:Spectrum Analysis, Raman; D015032:Zinc / Q000737:chemistry
D003300:Copper; D000426:Alcohol Dehydrogenase; D015032:Zinc