Crystal structure triosephosphate isomerase

Noble M E M, R K Wierenga, A-M Lambeir, F R Opperdoes, W H Thunnissen, K H Kalk, H Groendijk and W G J Hoi 1991. The Adaptability of the Active Site of Trypanosomal Triosephosphate Isomerase as Observed in the Crystal Structures of Three Different Complexes. Proteins Structure, Function and Genetics 10 50-69. 

D. Maes, J.P. Zeelen, N. Thanki, N. Beaucamp, M. Alvarez, M.H. Thi, J. Backmann, J.A. Martial, L. Wyns, R. Jaenicke, and R.K. Wierenga. 1999. The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima A comparative thermostability structural analysis of ten different TIM structures Proteins 37 441-453. (PubMed)... 

Mande SC, Mainfiroid V, Kalk KH, Goraj K, Martial JA, Hoi WG. Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosoma enzyme. Protein Sci 1994 3 810-21. 

The X-ray crystal structure of P. putida muconate lactonizing enzyme (cycloisomerase) was determined in 1987, and was found to contain an a/(i barrel fold, also found in triosephosphate isomerase and enolase. Remarkably, the structure of P. putida mandelate racemase, which catalyzes a mechanistically distinct reaction earlier in the same pathway, was found in 1990 to have a homologous structure, indicating that the structural fold of the enolase superfamily is able to support a range of enzyme-catalyzed reactions. The P. putida 3-carboxy- r, x-muconate lactonizing enzyme, in contrast, shares sequence similarity with a class II fumarase enzyme, and determination of its structure in 2004 has shown that it shares the same fold as the class II fumarase superfamily, hence these two catalysts of similar reactions have evolved from different ancestors. ... 

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