ライフサイエンスコーパス: hansenula

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1 spp., Geotrichum spp., 2 Hanseniaspora spp., Hansenula anomala, Hansenula wingei, 3 Rhodotorula spp.,

2 ndida (13 species), Cryptococcus neoformans, Hansenula anomala, Rhodotorula rubra, Saccharomyces cere

3 , 14 common and emerging species of Candida, Hansenula anomala, Rhodotorula spp., Saccharomyces cerev

4 Pichia pastoris (Pp) and Hansenula polymorpha (Hp) are methylotrophic yeasts comm

5 e cobalt substituted form of the enzyme from Hansenula polymorpha (HPAO) support pre-binding of molec

6 usly, using the amine oxidase from the yeast Hansenula polymorpha (HPAO), mutations of a strictly con

7 on has been further examined in the CAO from Hansenula polymorpha (HPAO).

8 ituted form of the copper amine oxidase from Hansenula polymorpha (HPAO).

9 idases and mutants of the amine oxidase from Hansenula polymorpha (HPAO).

10 a pair of copper amine oxidases (CAOs) from Hansenula polymorpha (HPAO-1 and HPAO-2).

11 res of copper amine oxidase-1 from the yeast Hansenula polymorpha (HPAO-1) in complex with ethylamine

12 f Cu(II)-dependent cofactor formation in the Hansenula polymorpha amine oxidase (HPAO) provided evide

13 tudy, we demonstrate that the apoform of the Hansenula polymorpha amine oxidase readily binds Cu(I) u

14 second-sphere ligand to the copper, D630N in Hansenula polymorpha amine oxidase, which greatly increa

15 ne-engineered strain of methylotrophic yeast Hansenula polymorpha and commercial urease is described.

16 The methylotrophic yeasts Hansenula polymorpha and Pichia pastoris are rapidly bec

17 gine was changed to an alanine in a CAO from Hansenula polymorpha expressed in Saccharomyces cerevisi

18 m of the copper amine oxidase from the yeast Hansenula polymorpha has been probed by site-directed mu

19 tudy, the structure of an amine oxidase from Hansenula polymorpha has been solved to 2.5 A resolution

20 ression of a copper amine oxidase (CAO) from Hansenula polymorpha in Saccharomyces cerevisiae under d

21 ration to the active site in the enzyme from Hansenula polymorpha is explored using a combination of

22 rosine Y305 in the copper amine oxidase from Hansenula polymorpha kinetically, spetroscopically, and,

23 In Hansenula polymorpha the 19-kb invertible region lies be

24 he active form of a yeast amine oxidase from Hansenula polymorpha, a hydrophobic space has been ident

25 s of a recombinant copper amine oxidase from Hansenula polymorpha, expressed in Saccharomyces cerevis

26 zyme alcohol oxidase obtained from the yeast Hansenula sp. which quantitatively produces acetaldehyde

27 p., 2 Hanseniaspora spp., Hansenula anomala, Hansenula wingei, 3 Rhodotorula spp., Saccharomyces cere

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