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Results 1 - 7 of 7
EC Number General Information Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.53physiological 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
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.53physiological 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
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.53physiological 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
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.53physiological function LPMO10 and a chitinase mutually enhance each otherย’s activities upon degrading chitin as the substrate -, 740398
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.53physiological function presence of CBP21 increases solubilization of chitin substrates with high degrees of crystallinity when combined with each of the three chitinases ChiA, ChiB, or ChiC, but this synergy is reduced upon decline in crystallinity 740562
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.53physiological function presence of LPMO10 increases the rate of chitin depolymerization by both chitinases ChiA and ChiB -, 740439
Display the word mapDisplay the reaction diagram Show all sequences 1.14.99.53physiological function the full-length enzyme and the individual catalytic LPMO module boost the activity of an endochitinase equally well, also yielding similar amounts of oxidized products. When grown on insoluble chitin substrates, the deletion mutant shows a reproducible growth defect on beta-chitin leading to an 2fold slower growth rate compared with the wild type strain. When grown on crab shells, the mutation leads to an extended lag phase of about 100 h 740758
Results 1 - 7 of 7