PMID- 16233797
OWN - NLM
STAT- MEDLINE
DCOM- 20051115
LR  - 20131121
IS  - 1389-1723 (Print)
IS  - 1347-4421 (Linking)
VI  - 99
IP  - 4
DP  - 2005 Apr
TI  - Hypothesis: structures, evolution, and ancestor of glucose kinases in the 
      hexokinase family.
PG  - 320-30
AB  - Glucose kinase, which we tentatively use in this review, represents the enzymes 
      catalyzing the phosphorylation of glucose and other hexoses by means of 
      phosphoryl donors (ATP, ADP, and inorganic polyphosphate [poly(P)]). Except for 
      glucose kinases utilizing ADP, all other glucose kinases belong to the hexokinase 
      (HK) family and are classified into three groups based on primary structural 
      information, i.e., groups HK, A, and B. The structural and evolutionary 
      relationships of glucose kinases belonging to the above three groups have been 
      controversial due to the lack of tertiary structural information on those in 
      groups A and B. However, recent studies on the tertiary structures of 
      poly(P)/ATP-glucomannokinase (GMK: a glucose kinase in group B) from Arthrobacter 
      sp. strain KM and glucokinase (GK) (ecoGK: a glucose kinase in group A) from 
      Escherichia coli have shed light on this problem. A comparison of the tertiary 
      structures of GMK and ecoGK with those of glucose kinases in group HK 
      demonstrated that both GMK and ecoGK are structurally homologous with glucose 
      kinases in group HK, and that glucose kinases belonging to groups HK, A, and B in 
      the HK family evolved divergently from a common ancestor. Based on the simple 
      structure of GMK compared to those of ecoGK and glucose kinases in group HK, and 
      the putative poly(P)-binding site in GMK, we propose that the ancestor of glucose 
      kinases in the HK family was similar to GMK and used poly(P). We also discuss the 
      ancestor and evolutionary process of ROK proteins, whose primary structures are 
      homologous with those of glucose kinases in group B, in connection with the 
      ancestor and evolutionary process of glucose kinases in the HK family.
FAU - Kawai, Shigeyuki
AU  - Kawai S
AD  - Department of Basic and Applied Molecular Biotechnology, Division of Food and 
      Biological Science, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 
      611-0011, Japan.
FAU - Mukai, Takako
AU  - Mukai T
FAU - Mori, Shigetarou
AU  - Mori S
FAU - Mikami, Bunzo
AU  - Mikami B
FAU - Murata, Kousaku
AU  - Murata K
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - Japan
TA  - J Biosci Bioeng
JT  - Journal of bioscience and bioengineering
JID - 100888800
RN  - 0 (Bacterial Proteins)
RN  - 0 (Hexoses)
RN  - EC 2.7.1.1 (Hexokinase)
RN  - IY9XDZ35W2 (Glucose)
SB  - IM
MH  - Amino Acid Sequence
MH  - Arthrobacter/enzymology/genetics
MH  - Bacterial Proteins/*chemistry/*genetics
MH  - Conserved Sequence
MH  - Escherichia coli/enzymology/genetics
MH  - *Evolution, Molecular
MH  - Glucose/*chemistry
MH  - Hexokinase/*chemistry/*genetics
MH  - Hexoses/*chemistry
MH  - Models, Genetic
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Conformation
MH  - Sequence Homology, Amino Acid
RF  - 39
EDAT- 2005/10/20 09:00
MHDA- 2005/11/16 09:00
CRDT- 2005/10/20 09:00
PHST- 2004/11/18 00:00 [received]
PHST- 2005/02/17 00:00 [accepted]
PHST- 2005/10/20 09:00 [pubmed]
PHST- 2005/11/16 09:00 [medline]
PHST- 2005/10/20 09:00 [entrez]
AID - S1389-1723(05)70374-1 [pii]
AID - 10.1263/jbb.99.320 [doi]
PST - ppublish
SO  - J Biosci Bioeng. 2005 Apr;99(4):320-30. doi: 10.1263/jbb.99.320.