Open AccessA single amine oxidase mediates utilization of primary aliphatic amines as nitrogen source by Kluyveromyces lactis
Author(s) -
Heath Lesley A.,
Large Peter J.
Publication year - 1984
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1984.tb00346.x
Subject(s) - methylamine , benzylamine , chemistry , yeast , biochemistry , methylamines , kluyveromyces lactis , amine oxidase , kluyveromyces , oxidase test , enzyme , stereochemistry , organic chemistry , saccharomyces cerevisiae
Yeasts of the genus Kluyveromyces grew very slowly on methylamine as sole nitrogen source. Methylamine oxidase activity in cell‐free extracts was very low. Under conditions known to separate methylamine oxidase from benzylamine oxidase in other yeast genera, only a single enzyme was detected in Kluyveromyces lactis . This enzyme could oxidize benzylamine, n ‐butylamine and (very poorly) methylamine. The enzyme lost no activity on heating at 45°C and had a high affinity and V max for benzylamine and 1‐aminoalkanes of long‐chain length, with a very low affinity and V max for methylamine. It is concluded that growth of K. lactis on methylamine involves only benzylamine oxidase, and that a methylamine oxidase of the type found in other yeasts does not occur.