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Primary structure of triosephosphate isomerase from Bacillus stearothermophilus.
1. Triosephosphate isomerase from Bacillus stearothermophilus is a dimeric enzyme comprising two chemically identical polypeptide chains. 2. The nearly complete amino acid sequence of the subunit polypeptide chain has been established from sequences of tryptic, chymotryptic and lysine-blocked tyrptic fragments of S-[2-14C]carboxymethylated enzyme. Overlaps not established by experimental data have been provisionally established from considerations of sequence homology with previously established sequences for the rabbit, chicken and coelacanth enzymes. The nearly complete sequence of the 249 residues is as follows. (See Text). 3. Comparison of the thermophile and chicken muscle enzymes shows that 40% of the residues are in identical sequence. 4. Correlation of the sequence of the thermophile enzyme with the three-dimensional structure of the muscle enzyme shows that residues in the catalytic site and in the subunit interface are strongly conserved. Possible correlations between sequence changes and thermal stabilisation of the dimeric structure are also noted.
PMID: 6105959 [PubMed - indexed for MEDLINE]
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Cited by 13 PubMed Central articles
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Plant Triose Phosphate Isomerase Isozymes : Purification, Immunological and Structural Characterization, and Partial Amino Acid Sequences.
Pichersky E, Gottlieb LD.
Plant Physiol. 1984 Feb; 74(2):340-347.
[Plant Physiol. 1984]
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Characterization of an intracellular oligopeptidase from Lactobacillus paracasei.
Tobiassen RO, Sørhaug T, Stepaniak L.
Appl Environ Microbiol. 1997 Apr; 63(4):1284-7.
[Appl Environ Microbiol. 1997]
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Human triosephosphate isomerase deficiency resulting from mutation of Phe-240.
Chang ML, Artymiuk PJ, Wu X, Hollán S, Lammi A, Maquat LE.
Am J Hum Genet. 1993 Jun; 52(6):1260-9.
[Am J Hum Genet. 1993]
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