Dihydroxyacetone kinase from a methylotrophic yeast, Hansenula polymorpha CBS 4732

1988 ◽  
Vol 150 (2) ◽  
pp. 155-159 ◽  
Author(s):  
Nobuo Kato ◽  
Hiroshi Yoshikawa ◽  
Katsuhiko Tanaka ◽  
Masayuki Shimao ◽  
Chikahiro Sakazawa
Keyword(s):  
Hansenula Polymorpha ◽  
Methylotrophic Yeast ◽  
Dihydroxyacetone Kinase

scholarly journals Watermelon glyoxysomal malate dehydrogenase is sorted to peroxisomes of the methylotrophic yeast, Hansenula polymorpha

FEBS Letters ◽  
1993 ◽  
Vol 334 (1) ◽  
pp. 128-132 ◽  
Author(s):  
I.J. van der Klei ◽  
K.N. Faber ◽  
I. Keizer-Gunnink ◽  
C. Gietl ◽  
W. Harder ◽  
...  
Keyword(s):  
Malate Dehydrogenase ◽  
Hansenula Polymorpha ◽  
Methylotrophic Yeast

scholarly journals Pyruvate Carboxylase Is an Essential Protein in the Assembly of Yeast Peroxisomal Oligomeric Alcohol Oxidase

2003 ◽  
Vol 14 (2) ◽  
pp. 786-797 ◽  
Author(s):  
Paulina Ozimek ◽  
Ralf van Dijk ◽  
Kantcho Latchev ◽  
Carlos Gancedo ◽  
Dong Yuan Wang ◽  
...  
Keyword(s):  
Pyruvate Carboxylase ◽  
Tricarboxylic Acid Cycle ◽  
Hansenula Polymorpha ◽  
Alcohol Oxidase ◽  
Methylotrophic Yeast ◽  
Tricarboxylic Acid ◽  
Matrix Proteins ◽  
Growth Media ◽  
Fad Binding

Hansenula polymorpha ass3 mutants are characterized by the accumulation of inactive alcohol oxidase (AO) monomers in the cytosol, whereas other peroxisomal matrix proteins are normally activated and sorted to peroxisomes. These mutants also have a glutamate or aspartate requirement on minimal media. Cloning of the corresponding gene resulted in the isolation of the H. polymorpha PYC gene that encodes pyruvate carboxylase (HpPyc1p). HpPyc1p is a cytosolic, anapleurotic enzyme that replenishes the tricarboxylic acid cycle with oxaloacetate. The absence of this enzyme can be compensated by addition of aspartate or glutamate to the growth media. We show that HpPyc1p protein but not the enzyme activity is essential for import and assembly of AO. Similar results were obtained in the related yeast Pichia pastoris. In vitro studies revealed that HpPyc1p has affinity for FAD and is capable to physically interact with AO protein. These data suggest that in methylotrophic yeast pyruvate carboxylase plays a dual role in that, besides its well-characterized metabolic function as anapleurotic enzyme, the protein fulfils a specific role in the AO sorting and assembly process, possibly by mediating FAD-binding to AO monomers.

Development of the Thermotolerant Methylotrophic Yeast Hansenula polymorpha as Efficient Ethanol Producer

2017 ◽  
pp. 257-282 ◽  
Author(s):  
Kostyantyn Dmytruk ◽  
Olena Kurylenko ◽  
Justyna Ruchala ◽  
Olena Ishchuk ◽  
Andriy Sibirny
Keyword(s):  
Hansenula Polymorpha ◽  
Methylotrophic Yeast ◽  
Ethanol Producer
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