Alcohol Oxidases of Kloeckera sp. and Hansenula polymorpha. Catalytic Properties and Subunit Structures
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چکیده
منابع مشابه
In vitro dissociation and re-assembly of peroxisomal alcohol oxidases of Hansenula polymorpha and Pichia pastoris.
We have studied the in vitro inactivation/dissociation and subsequent reactivation/re-assembly of peroxisomal alcohol oxidases (AO) from the yeasts Hansenula polymorpha and Pichia pastoris. Both proteins are homo-oligomers consisting of eight identical subunits, each containing one FAD as the prosthetic group. They were both rapidly inactivated upon incubation in 80% glycerol, due to their diss...
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Telomerase is a ribonucleoprotein, the main function of which is to synthesize telomeres, i.e. repetitive sequences which are localized at the ends of eukaryotic chromosomes. Telomerase maintains the stability of the genome in eukaryotic cells by replicating chromosomal ends. The structural and functional investigation of the telomerase complex is significantly restricted due to difficulties co...
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The structural underpinnings of enzyme substrate specificity are investigated in a pair of copper amine oxidases (CAOs) from Hansenula polymorpha (HPAO-1 and HPAO-2). The X-ray crystal structure (to 2.0 A resolution) and steady state kinetic data of the second copper amine oxidase (HPAO-2) are presented for comparison to those of HPAO-1. Despite 34% sequence identity and superimposable active s...
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In the yeast Hansenula polymorpha the development and turnover of peroxisomes is readily achieved by manipulation of the cultivation conditions. The organelles massively develop when the cells are incubated in the presence of methanol as the sole source of carbon and energy. However, they are rapidly and selectively degraded when methanol-grown cells are placed at conditions of repression of me...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1976
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1976.tb10307.x