PMID- 9100345
OWN - NLM
STAT- MEDLINE
DCOM- 19970513
LR  - 20190909
IS  - 0273-2289 (Print)
IS  - 0273-2289 (Linking)
VI  - 61
IP  - 1-2
DP  - 1996 Oct-Nov
TI  - Thermostability of yeast hexokinase and yeast glucose-6-phosphate dehydrogenase.
PG  - 67-74
AB  - Kinetic study of the mechanism of the temperature-induced loss of the catalytic 
      activity by yeast hexokinase (HK) and yeast glucose-6-phosphate dehydrogenase 
      (G-6-PDG) has shown the dissociative nature of the processes. In the temperature 
      range 40-47 degrees C, they are satisfactorily described in terms of consecutive 
      reactions in which steps of irreversible denaturation of the monomeric units 
      follow the reversible dissociation of inactive oligomeric forms into the active 
      units, resulting in an increase in catalytic activity. The experimental data have 
      been analyzed in the framework of the dissociative mechanism, and a 
      semiquantitative method has been developed for calculating the individual rate 
      constants.
FAU - Zaitzeva, E A
AU  - Zaitzeva EA
AD  - M. V. Lomonosov Moscow State University, Department of Chemistry, Russia.
FAU - Chukrai, E S
AU  - Chukrai ES
FAU - Poltorak, O M
AU  - Poltorak OM
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Appl Biochem Biotechnol
JT  - Applied biochemistry and biotechnology
JID - 8208561
RN  - EC 1.1.1.49 (Glucosephosphate Dehydrogenase)
RN  - EC 2.7.1.1 (Hexokinase)
SB  - IM
MH  - Enzyme Stability
MH  - Glucosephosphate Dehydrogenase/*metabolism
MH  - Hexokinase/*metabolism
MH  - Hot Temperature
MH  - Kinetics
MH  - Yeasts/enzymology
EDAT- 1996/10/01 00:00
MHDA- 1996/10/01 00:01
CRDT- 1996/10/01 00:00
PHST- 1996/10/01 00:00 [pubmed]
PHST- 1996/10/01 00:01 [medline]
PHST- 1996/10/01 00:00 [entrez]
AID - 10.1007/BF02785689 [doi]
PST - ppublish
SO  - Appl Biochem Biotechnol. 1996 Oct-Nov;61(1-2):67-74. doi: 10.1007/BF02785689.