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Literature summary for 5.3.1.1 extracted from

  • Thanki, N.; Zeelen, J.P.; Mathieu, M.; Jaenicke, R.; Abagyan, R.A.; Wierenga, R.K.; Schliebs, W.
    Protein Engineering with monomeric triosephosphate isomerase (monoTIM): the modelling and structure verification of a seven-residue loop (1997), Protein Eng., 10, 159-167.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
genetically engineered enzyme variant, at 2.6 A resolution Trypanosoma sp.

Protein Variants

Protein Variants Comment Organism
additional information construction of a monomeric enzyme form with loop-1 one residue shorter than monoTIM, which is constructed by replacing 15 residues of the major interface loop by another 8-residue fragment. The catalytic activity and stability of the new seven-residue Loop-1 enzyme variant is similar with that of monoTIM Trypanosoma sp.

Organism

Organism UniProt Comment Textmining
Trypanosoma sp.
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-
-

Purification (Commentary)

Purification (Comment) Organism
genetically engineered enzyme variant Trypanosoma sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Glyceraldehyde 3-phosphate
-
Trypanosoma sp. Glycerone phosphate
-
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