Identification and characterization of an ATP-dependent hexokinase with broad substrate specificity from the hyperthermophilic archaeon Sulfolobus tokodaii.
As a new member of the glucose-phosphorylating enzymes, the ATP-dependent hexokinase from the hyperthermophilic crenarchaeon Sulfolobus tokodaii was purified, identified, and characterized. Our results revealed that the enzyme differs from other known enzymes in primary structure and its broad substrate specificity for both phosphoryl donors and acceptors.
Department of Biotechnology, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Hiroshi
H
Nishimasu
Shinya
S
Fushinobu
Hirofumi
H
Shoun
Takayoshi
T
Wakagi
D000255:Adenosine Triphosphate; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D005947:Glucose / Q000378:metabolism; D006593:Hexokinase / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011994:Recombinant Proteins / Q000378:metabolism; D016415:Sequence Alignment; D013045:Species Specificity; D013379:Substrate Specificity; D016944:Sulfolobus / Q000201:enzymology*
D019843:Archaeal Proteins; D011994:Recombinant Proteins; D000255:Adenosine Triphosphate; D006593:Hexokinase; D005947:Glucose