Characterization of the Hansenula polymorpha CPY gene encoding carboxypeptidase Y

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Characterization of the Hansenula polymorpha CPY gene encoding carboxypeptidase Y.

We have isolated the Hansenula polymorpha CPY gene encoding carboxypeptidase Y (Hp-CPY). The deduced amino acid sequence revealed that Hp-CPY consists of 541 amino acids and has a calculated Mr of 60,793. The protein is highly similar to Saccharomyces cerevisiae CPY (61.8% identity). At the N-terminus of Hp-CPY signals for the entry into the secretory pathway and subsequent sorting to the vacuo...

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Characterization of the Hansenula polymorpha CPY gene encoding carboxypeptidase

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Richard J. S. Baerends,{, Grietje J. Sulter, Thomas W. Jeffries, James M. Cregg and Marten Veenhuis* 1 Eukaryotic Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands 2 Institute for Microbial and Biochemical Technology, Forest Products Laboratory, US Department of Agriculture, One Gifford Pinchot Drive, ...

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Molecular characterization of the Hansenula polymorpha FLD1 gene encoding formaldehyde dehydrogenase.

Glutathione-dependent formaldehyde dehydrogenase (FLD) is a key enzyme required forthe catabolism of methanol as a carbon source and certain primary amines, such as methylamine as nitrogen sources in methylotrophic yeasts. Here we describe the molecular characterization of the FLD1 gene from the yeast Hansenula polymorpha. Unlike the recently described Pichia pastoris homologue, the H. polymorp...

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ژورنال

عنوان ژورنال: Yeast

سال: 1999

ISSN: 0749-503X,1097-0061

DOI: 10.1002/(sici)1097-0061(199902)15:3<181::aid-yea355>3.3.co;2-p