A calcium-dependent xylan-binding domain of alkaline xylanase from alkaliphilic Bacillus sp. strain 41M-1. 2011

Risa Yazawa, and Jun Takakura, and Tomoko Sakata, and Ihsanawati, and Rie Yatsunami, and Toshiaki Fukui, and Takashi Kumasaka, and Nobuo Tanaka, and Satoshi Nakamura
Department of Bioengineering, Tokyo Institute of Technology, Yokohama, Japan.

Xylanase J of alkaliphilic Bacillus sp. strain 41M-1 contains a carbohydrate-binding module family 36 xylan-binding domain (XBD). Mutational analysis of the XBD revealed that Tyr237, Asp313, Trp317, and Asp318 were involved in Ca(2+)-dependent xylan-binding, and that Asp313 and Asp318 were especially important.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
D002118 Calcium A basic element found in nearly all tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes. Coagulation Factor IV,Factor IV,Blood Coagulation Factor IV,Calcium-40,Calcium 40,Factor IV, Coagulation
D001407 Bacillus A genus of BACILLACEAE that are spore-forming, rod-shaped cells. Most species are saprophytic soil forms with only a few species being pathogenic. Bacillus bacterium
D014990 Xylans Polysaccharides consisting of xylose units. Xylan
D017434 Protein Structure, Tertiary The level of protein structure in which combinations of secondary protein structures (ALPHA HELICES; BETA SHEETS; loop regions, and AMINO ACID MOTIFS) pack together to form folded shapes. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Tertiary Protein Structure,Protein Structures, Tertiary,Tertiary Protein Structures
D043364 Endo-1,4-beta Xylanases Enzymes which catalyze the endohydrolysis of 1,4-beta-D-xylosidic linkages in XYLANS. Endo-1,4-beta-Xylanase,1,4-beta-D-Xylanohydrolase,Beta-1-4-Endoxylanase,Endo-1,4-Xylanase II,Endo-1,4-beta-Xylanase II,Endoxylanase,Xylanase A,Xylanase B,Xylanase C,Xylanase D,Xylanase J,Xylanase Y,Xylanase Z,beta Xylanase,1,4 beta D Xylanohydrolase,Beta 1 4 Endoxylanase,Endo 1,4 Xylanase II,Endo 1,4 beta Xylanase,Endo 1,4 beta Xylanase II,Endo 1,4 beta Xylanases,Xylanase, beta,Xylanases, Endo-1,4-beta

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