[Biochemical response of recombinant Hansenula polymorpha strains to oversynthesis of homologous dioxyacetone kinase and bacterial beta-galactosidase].
Changes in the activities of key enzymes responsible for utilization of methanol by recombinant strains of methylotrophic yeasts H. polymorpha R22-2B and H. polymorpha LAC-56 grown in a chemostat are described. The strain R22-2B displaying a high activity of dioxyacetone kinase had also a high activity of formaldehyde dehydrogenase, which increased the rate of dissimilation of formaldehyde. There was a decrease in ATP concentration in the strain LAC-56 oversynthesizing beta-galactosidase from Escherichia coli; this effect decreased the rate of assimilation of formaldehyde.
Vel'kov
V V
VV
Matys
V Iu
VIu
Sokolov
D M
DM
D000255:Adenosine Triphosphate / Q000378:metabolism; D000445:Aldehyde Oxidoreductases / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D005557:Formaldehyde / Q000378:metabolism; D005991:Glycerol Kinase / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism; D010843:Pichia / Q000235:genetics / Q000378:metabolism*; D011995:Recombination, Genetic; D001616:beta-Galactosidase / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism
D005557:Formaldehyde; D000255:Adenosine Triphosphate; C020145:formaldehyde dehydrogenase (glutathione); D000445:Aldehyde Oxidoreductases; D005991:Glycerol Kinase; D001616:beta-Galactosidase