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Xyl10A is a modular enzyme consisting of an N-terminal catalytic domain and CBM1 separated by a Ser/Thr-rich linker region [ 19].
The predicted MeCbl chemistry of class B bears some similarity with that catalyzed by the cobalamin-dependent methionine synthase, MetH, which is a modular enzyme consisting of four distinct domains.
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SaAraf43A provides a good model for investigating the hydrolytic activity of the modular enzyme.
Cystathionine β-synthase (CBS) is a modular enzyme which catalyzes condensation of serine with homocysteine.
SaAraf43A is a modular enzyme possessing CBM42 at its C terminus.
Studies in this area have largely focused on modular enzyme systems, such as those encoding non-ribosomal peptides and polyketides.
Thermostable endo-β-1,4-xylanase (Xyl10A) from Talaromyces cellulolyticus, which is recognized as one of the core enzymes in the fungal cellulase system, has a modular structure consisting of a glycoside hydrolase family 10 catalytic domain and CBM1 at the C-terminus separated by a linker region.
A modular model, consisting of three sub-models is presented.
It has a modular structure consisting of five basic, six fundamental and four applied modules.
The PETSAT proposal is for a modular satellite consisting of any number of unfolding functional panels.
SF2/ASF exhibits a modular structure consisting of two copies of RNA binding motifs (RRM1 and RRM2), followed by an arginine-serine rich (RS) domain [21].
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