PMID- 19558793
OWN - NLM
STAT- MEDLINE
DCOM- 20090812
LR  - 20220409
IS  - 1976-6696 (Print)
IS  - 1976-6696 (Linking)
VI  - 42
IP  - 6
DP  - 2009 Jun 30
TI  - Enzymatic properties of the N- and C-terminal halves of human hexokinase II.
PG  - 350-5
AB  - Although previous studies on hexokinase (HK) II indicate both the N- and 
      C-terminal halves are catalytically active, we show in this study the N-terminal 
      half is significantly more catalytic than the C-terminal half in addition to 
      having a significantly higher Km for ATP and Glu. Furthermore, truncated forms of 
      intact HK II lacking its first N-terminal 18 amino acids (delta18) and a 
      truncated N-terminal half lacking its first 18 amino acids (delta18N) have higher 
      catalytic activity than other mutants tested. Similar results were obtained by 
      PET-scan analysis using (18)FFDG. Our results collectively suggest that each 
      domain of HK II possesses enzyme activity, unlike HK I, with the N-terminal half 
      showing higher enzyme activity than the C-terminal half.
FAU - Ahn, Keun Jae
AU  - Ahn KJ
AD  - Division of Nuclear Medicine, Department of Diagnostic Radiology, Research 
      Institute of Radiological Science, Yonsei University College of Medicine, Seoul 
      120-752, Korea.
FAU - Kim, Jongsun
AU  - Kim J
FAU - Yun, Mijin
AU  - Yun M
FAU - Park, Jeon Han
AU  - Park JH
FAU - Lee, Jong Doo
AU  - Lee JD
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Korea (South)
TA  - BMB Rep
JT  - BMB reports
JID - 101465334
RN  - 0 (Isoenzymes)
RN  - 0 (Mutant Proteins)
RN  - EC 2.7.1.1 (Hexokinase)
SB  - IM
MH  - Catalysis
MH  - Catalytic Domain
MH  - Hexokinase/*chemistry/*metabolism
MH  - Humans
MH  - Isoenzymes/metabolism
MH  - Kinetics
MH  - Mutant Proteins/metabolism
MH  - Protein Structure, Tertiary/physiology
MH  - Tumor Cells, Cultured
EDAT- 2009/06/30 09:00
MHDA- 2009/08/13 09:00
CRDT- 2009/06/30 09:00
PHST- 2009/06/30 09:00 [entrez]
PHST- 2009/06/30 09:00 [pubmed]
PHST- 2009/08/13 09:00 [medline]
AID - 10.5483/bmbrep.2009.42.6.350 [doi]
PST - ppublish
SO  - BMB Rep. 2009 Jun 30;42(6):350-5. doi: 10.5483/bmbrep.2009.42.6.350.