Cutinase structure

Carvalho CML, Aires-Barros MR, Cabral IMS (1998) Cutinase structure, function and biocat-alytic applications. Electron J Biotechnol 1 160-173... 

Carvalho, C.M.L., Aires-Barros, M.R., and Cabral, J.M.S. (1998) Cutinase structure, function and biocatalytic applications. Electron./. Biotechnol,... 

Carvalho, C. M. L. C., M. R. Aires-Barro, and J. M. S. Cabral. 1998. Cutinase Structure, Function and Biocatalytic Applications. Electronic Journal of Biotechnology 1 160-173. 

The crystal structure of cutinase from F. solani f. pisi (Fig. 10) indicated that this fungal cutinase constitutes a separate class of enzyme that maybe regarded as a bridge between esterases and lipases in that the free cutinase has a well-de-... 

Fig. 10. Structure ofF. solani tpisi cutinase expressed in E. coli [121]. Locations of active site residues are indicated...

The conversion of the kinetic data into AAG -values (Table 4.2) assumes that the rate-limiting step is the same in wild type and variant. It also assumes that the mutation does not cause structural rearrangements. Only in very few cases have the kinetic studies on the transition state stabilization by the oxyanion hole contributions been complemented by protein crystallographic studies of the liganded wild-type and mutated variant. One such example, discussed in more detail below, concerns the studies on the Ser42Ala variant of cutinase, in which case it was found that the structural changes are minimal [19]. 

Figure 4.4 Structure of the oxyanion hole of cutinase, with a covalently bound transition state analog, diethyl phosphate (PDB 2CUT).

AOT/isooctane Recombinant Cutinase Fluorescence study of cutinase in RMs to evaluate its structure and protein unfolding [54]... 

Figure 3-22 Stereoscopic view of a section of the structure of cutinase from the fungus Fusarium solani determined to a resolution of 0.10 nm. The three amino acid residues shown are serine 120 (top), histidine 188, and aspartate 175 (lower left). The structure is presented as a contour map with a "wire mesh" drawn at a "cutoff" level of density equal to 1 a above the average, where a is the root mean square density of the entire map. The side chains of these three residues constitute the "catalytic triad" in the active site of this enzyme (see Chapter 12). At this resolution more than one conformation of a group may often be seen. For example, the gamma oxygen (OG) of S120 is seen in two positions, the major one being toward His 188. When the map is drawn with a lower contour level the N-H proton on His 188 that is hydrogen bonded to Asp 175 can also be seen.410 Courtesy of Christian Cambillau.

Thiosulfate cyanide sulfurtransferase symmetry in 78 TTiiouridine 234 Three-dimensional structures of aconitase 689 adenylate kinase 655 aldehyde oxido-reductase 891 D-amino acid oxidase 791 a-amylase, pancreatic 607 aspartate aminotransferase 57,135 catalytic intermediates 752 aspartate carbamyltransferase 348 aspartate chemoreceptor 562 bacteriophage P22 66 cadherin 408 calmodulin 317 carbonic acid anhydrase I 679 carboxypeptidase A 64 catalase 853 cholera toxin 333, 546 chymotrypsin 611 citrate synthase 702, 703 cutinase 134 cyclosporin 488 cytochrome c 847 cytochrome c peroxidase 849 dihydrofolate reductase 807 DNA 214, 223,228,229, 241 DNA complex... 

An MD study of an enzyme, the serine protease cutinase from Fusarium solani pisi, in [C4mim][PF6] and [C4mim][N03] was presented. The authors observed an enzyme structure that is dependent on the amount of water present in the IL [124], They showed that the enzyme is preferentially stabilized in [C4mim][PF6] at 5-10 wt% (weight of water over protein) water content at 298 K. [C4mim][PF6] rendered a more native-like enzyme structure at the same water content of 5—10 wt% as... 

Figure 15.1 Surface structure of PTT fibers (a) after hydrolysis with NaOH and (b) with the T.fusca cutinase leading to similar increase in surface hydrophilicity.(Reproduced with permission from [56]. Copyright (2008) Elsevier).

Figure 15.3 Detail of the active site X-ray structure of cutinase with the energy minimized structure of the Tl of (a) 1,2-ethanodiol dibenzoate (PET model substrate) and (b) PA 6,6. The catalytic...

The structure of the cutinase gene has been determined using genomic DNA cloned in X-phage. This gene contains one 51 bp intron which has the typical junction and splicing signals... 

Figure 2. Nucleotide sequence of the cloned cutinase cDNA and the amino acid sequence deduced from it, C-4 and C-57 indicate the beginning of the nucleotide sequence of two additional cDNA clones. The solid lines represent the regions for which the primary structure was confirmed by amino acid sequencing.

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