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The several catalytic modules on the same polypeptide chain are assembled such that their enforced proximity account for an enhanced concerted action on substrates (Moraïs et al. 2012).
The presence of several catalytic modules in the same polypeptide chain would seem to indicate that their enforced proximity would account for an enhanced concerted action on cellulosic substrates.
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ORFs that include GH10 or GH11 xylanase modules commonly showed multiple catalytic modules.
This revealed the presence of multiple catalytic modules in xylanases [19], [20], [21] and the presence of non-catalytic dockerins [19], [22] and of substrate-binding modules [23] in both cellulases and xylanases.
These dockerin-containing ORFs encode a variety of catalytic modules including glycoside hydrolases (GHs), polysaccharide lyases, and carbohydrate esterases.
Thus for the six completed ORFs that include a GH5 module, and the four completed ORFs that include a GH9 module, these were the only identified catalytic module present, as opposed to some examples of multiple catalytic modules that occur in GH9 and GH5 enzymes of the Clostridium thermocellum cellulosome.
In contrast to the situation with polypeptides that carry GH10 and GH11 xylanase modules (Figure 3), there were rather few instances where GH5 or GH9 modules were combined with other catalytic modules in the same polypeptide.
Catalytic modules are marked in bold.
They are modular proteins composed of catalytic modules and sometimes a noncatalytic carbohydrate-binding module.
Briefly, sequences of the proteins in CAZy were first divided by their constitutive modules (catalytic modules, carbohydrate binding module and other noncatalytic modules).
For half of the catalytic modules (53/118), the number of modules was identical in all six isolates.
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