ChemInform Abstract: Structural Analysis of a Stereochemical Modification of Flavin Adenine Dinucleotide in Alcohol Oxidase from Methylotrophic Yeasts.

ChemInform ◽  
2010 ◽  
Vol 23 (36) ◽  
pp. no-no
Author(s):  
R. M. KELLOGG ◽  
W. KRUIZINGA ◽  
L. V. BYSTRYKH ◽  
L. DIJKHUIZEN ◽  
W. HARDER
Keyword(s):  
Structural Analysis ◽  
Flavin Adenine Dinucleotide ◽  
Alcohol Oxidase ◽  
Methylotrophic Yeasts

Structural analysis of a stereochemical modification of flavin adenine dinucleotide in alcohol oxidase from methylotrophic yeasts

Tetrahedron ◽  
1992 ◽  
Vol 48 (20) ◽  
pp. 4147-4162 ◽  
Author(s):  
Richard M Kellogg ◽  
Wim Kruizinga ◽  
Leonid V Bystrykh ◽  
Lubbert Dijkhuizen ◽  
Wim Harder
Keyword(s):  
Structural Analysis ◽  
Flavin Adenine Dinucleotide ◽  
Alcohol Oxidase ◽  
Methylotrophic Yeasts

Isolation of alcohol oxidase and two other methanol regulatable genes from the yeast Pichia pastoris

1985 ◽  
Vol 5 (5) ◽  
pp. 1111-1121
Author(s):  
S B Ellis ◽  
P F Brust ◽  
P J Koutz ◽  
A F Waters ◽  
M M Harpold ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Carbon Source ◽  
Sole Carbon Source ◽  
Alcohol Oxidase ◽  
Methylotrophic Yeasts ◽  
Sequence Analyses ◽  
Yeast Pichia Pastoris ◽  
Oxidation Of Methanol ◽  
Regulated Expression

The oxidation of methanol follows a well-defined pathway and is similar for several methylotrophic yeasts. The use of methanol as the sole carbon source for the growth of Pichia pastoris stimulates the expression of a family of genes. Three methanol-responsive genes have been isolated; cDNA copies have been made from mRNAs of these genes, and the protein products from in vitro translations have been examined. The identification of alcohol oxidase as one of the cloned, methanol-regulated genes has been made by enzymatic, immunological, and sequence analyses. Methanol-regulated expression of each of these three isolated genes can be demonstrated to occur at the level of transcription. Finally, DNA subfragments of two of the methanol-responsive genomic clones from P. pastoris have been isolated and tentatively identified as containing the control regions involved in methanol regulation.

scholarly journals Flavin adenine dinucleotide binding is the crucial step in alcohol oxidase assembly in the yeast Hansenula polymorpha

Yeast ◽  
1996 ◽  
Vol 12 (10) ◽  
pp. 917-923 ◽  
Author(s):  
Melchior E. Evers ◽  
Vladimir Titorenko ◽  
Wim Harder ◽  
Ida van der Klei ◽  
Marten Veenhuis
Keyword(s):  
Flavin Adenine Dinucleotide ◽  
Hansenula Polymorpha ◽  
Alcohol Oxidase ◽  
Crucial Step

Distribution, diversity and regulation of alcohol oxidase isozymes, and phylogenetic relationships of methylotrophic yeasts

Yeast ◽  
2007 ◽  
Vol 24 (6) ◽  
pp. 523-532 ◽  
Author(s):  
Takashi Ito ◽  
Shuki Fujimura ◽  
Masataka Uchino ◽  
Naoto Tanaka ◽  
Yoshimi Matsufuji ◽  
...  
Keyword(s):  
Phylogenetic Relationships ◽  
Alcohol Oxidase ◽  
Methylotrophic Yeasts

scholarly journals Structural Analysis of Flavinylation in Vanillyl-Alcohol Oxidase

2000 ◽  
Vol 275 (49) ◽  
pp. 38654-38658 ◽  
Author(s):  
Marco W. Fraaije ◽  
Robert H. H. van den Heuvel ◽  
Willem J. H. van Berkel ◽  
Andrea Mattevi
Keyword(s):  
Structural Analysis ◽  
Alcohol Oxidase ◽  
Vanillyl Alcohol ◽  
Vanillyl Alcohol Oxidase

scholarly journals Assembly of alcohol oxidase in peroxisomes of the yeast Hansenula polymorpha requires the cofactor flavin adenine dinucleotide.

1994 ◽  
Vol 5 (8) ◽  
pp. 829-837 ◽  
Author(s):  
M E Evers ◽  
V I Titorenko ◽  
I J van der Klei ◽  
W Harder ◽  
M Veenhuis
Keyword(s):  
Molecular Chaperone ◽  
Matrix Protein ◽  
Protein Import ◽  
Flavin Adenine Dinucleotide ◽  
Hansenula Polymorpha ◽  
Alcohol Oxidase ◽  
Auxotrophic Mutant ◽  
Matrix Proteins ◽  
Wild Type ◽  
Wild Type Control

The peroxisomal flavoprotein alcohol oxidase (AO) is an octamer (600 kDa) consisting of eight identical subunits, each of which contains one flavin adenine dinucleotide molecule as a cofactor. Studies on a riboflavin (Rf) auxotrophic mutant of the yeast Hansenula polymorpha revealed that limitation of the cofactor led to drastic effects on AO import and assembly as well as peroxisome proliferation. Compared to wild-type control cells Rf-limitation led to 1) reduced levels of AO protein, 2) reduced levels of correctly assembled and activated AO inside peroxisomes, 3) a partial inhibition of peroxisomal protein import, leading to the accumulation of precursors of matrix proteins in the cytosol, and 4) a significant increase in peroxisome number. We argue that the inhibition of import may result from the saturation of a peroxisomal molecular chaperone under conditions that normal assembly of a major matrix protein inside the target organelle is prevented.

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