A coleopteran triosephosphate isomerase: X-ray structure and phylogenetic impact of insect sequences.
A coleopteran triosephosphate isomerase (TIM) from Tenebrio molitor (yellow mealworm beetle) was recombinantly expressed in Escherichia coli and characterized with respect to thermal stability, kinetic parameters and oligomeric state. The enzyme was successfully crystallized and the structure determined by X-ray analysis to 2.0 A resolution. This is the first example of an invertebrate TIM. We compare structural features with known structures of TIMs from microorganisms, plants and vertebrates, and discuss the utility of the Tenebrio TIM sequence, together with several newly sequenced insect TIMs, for molecular phylogenetic analysis.
Knobeloch
D
D
Institut für Biochemie, Charité- Universitätsmedizin Berlin, Berlin.
Schmidt
A
A
Scheerer
P
P
Krauss
N
N
Wessner
H
H
Scholz
Ch
Ch
Küttner
G
G
von Rintelen
T
T
Wessel
A
A
Höhne
W
W
D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray; D006801:Humans; D019476:Insect Proteins / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D017422:Sequence Analysis, DNA; D013712:Tenebrio / Q000201:enzymology*; D014305:Triose-Phosphate Isomerase / Q000737:chemistry / Q000378:metabolism*
D019476:Insect Proteins; D014305:Triose-Phosphate Isomerase