EC Number   |
General Information   |
Reference   |
|---|
 1.14.99.53 | metabolism |
enzyme has two carbohydrate-binding modules, CBM5 and CBM73. Both CBMs bind crystalline chitin with Kd values in the micromolar range, CBM73 has higher affinity for chitin than CjCBM5. CBM5 binds soluble chitohexaose, whereas no binding of CBM73 chitohexaose is detected. In CBM5, conserved aromatic amino acids involved in substrate binding residues show a linear arrangement that seems compatible with the experimentally observed affinity for single chitin chains. The arrangement of these residues in CBM73 suggests a wider binding surface that may interact with several chitin chains |
-, 767133 |
 1.14.99.53 | metabolism |
role of LPMO's structural dynamics during polysaccharide degradation, comparison of multiple LPMO structures. The substrate binding region is highly flexible with significant and sustained micro-scale level conformational changes.The loops on the binding side of the substrate are most mobile, in concert with the dynamic modes influencing the motions during binding. There are dynamic differences between families AA9, AA10, AA11, and AA13 that consist of more than one structure. The patterns of motion in the loop regions among the AA9 structures are distinct from those in the AA10 structures |
767309 |
 1.14.99.53 | physiological function |
cellobiose dehydrogenase from Myriococcum thermophilum can act as an electron donor. Employing the enzyme as electron donor enables a kinetically controlled supply of electrons to the LPMO. The rate of chitin oxidation by CBP21 is equal to that of cosubstrate (lactose) oxidation by cellobiose dehydrogenase, verifying the usage of two electrons in the LPMO catalytic mechanism. Lactose oxidation correlates directly with the rate of LPMO catalysis, a method for indirect determination of LPMO activity is implicated |
-, 741377 |
 1.14.99.53 | physiological function |
deletion of cbpD renders Pseudomonas aeruginosa unable to establish a lethal systemic infection, associated with enhanced bacterial clearance in vivo. CbpD-dependent survival of the wild-type bacterium is not attributable to dampening of pro-inflammatory responses by CbpD ex vivo or in vivo. CbpD attenuates the terminal complement cascade in human serum. Catalytic activity is crucial for virulence function. The lack of the enzyme result in substantial reorganization of the bacterial and host proteomes |
-, 767577 |
 1.14.99.53 | physiological function |
downregulation of LPMO15-3 expression at the 4th or 5th instar nymph stage severely decreases the survival rate and results in lethal phenotypes. The deficient individuals exhibit incompletely digested peritrophic matrix |
766913 |
 1.14.99.53 | physiological function |
enzyme increases chitin solubilization yields of chitinases by up to 30fold and 20fold for alpha- and beta-chitin, respectively. The addition of LPMO10F leads to a substantial increase in the (GlcNAc)2:GlcNAc product ratio of chitinases, in reactions with alpha-chitin only |
-, 740434 |
 1.14.99.53 | physiological function |
enzyme produces oxidized cello-oligosaccharides from cellulose and boosts cellulose degradation by cellulases. The binding ability of LPMO10A depends on carbohydrate binding module CBM2 |
-, 766932 |
 1.14.99.53 | physiological function |
in presence of lytic polysaccharide monooxygenase Cbp21, the apparent kcat values of chitinases ChiA and ChiB increase 6-9fold, while there is no effect on chitinase ChiC |
740261 |
 1.14.99.53 | physiological function |
LPMO10 and a chitinase mutually enhance each otherยs activities upon degrading chitin as the substrate |
-, 740398 |
 1.14.99.53 | physiological function |
member of lytic polysaccharide monooxygenase family AA11 |
-, 766874 |