EC Number   |
Substrates |
Products  |
Reversibility |
|---|
   1.14.99.53 | more |
data indicate that catalysis involves equatorial binding of a reactive oxygen species |
? |
- |
? |
| 1.14.99.53 | more |
the enzyme produces oxidized chitin oligosaccharides with a degree of polymerization from DPox3 to DPox11. The relative intensities of DPox4, DPox6, DPox8 and DPox10 are remarkably higher than DPox5, DPox7, DPox9 and DPox11. LPMO10A shows little binding to Avicel |
? |
- |
? |
| 1.14.99.53 | more |
no activity on other substrates including diverse mannans, cellulose and starch |
? |
- |
? |
| 1.14.99.53 | more |
enzyme in presence of ascorbate but lacking chitin produces H2O2 |
? |
- |
? |
| 1.14.99.53 | more |
mechanistic model, copper is reduced on the enzyme by an externally provided electron and followed by oxygen binding and activation by internal electron transfer. Substrate binding involves an extended planar binding surface, including the metal binding site. Chitin binding protects two regions from 2H/1H exchange, Gln53-Ser58 and Leu110-Thr116 |
? |
- |
? |
| 1.14.99.53 | more |
isoform LPMO10B produces C4-oxidized (4-ketoaldoses) and double (C4/C1)-oxidized cello-oligosaccharides. No substrate: alpha-chitin |
? |
- |
? |
| 1.14.99.53 | more |
enzyme binds to cellulose, but does not display catalyic activity |
? |
- |
? |
| 1.14.99.53 | more |
the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved |
? |
- |
? |
| 1.14.99.53 | more |
[(1->4)-N-acetyl-beta-D-glucosaminyl]6 is a substrate, but not shorter oligomers |
? |
- |
? |
| 1.14.99.53 | more |
presence of ascorbate is required. No substrates: phosphoric acid-swollen cellulose, avicel, tamarind xyloglucan, birchwood xylan, beechwood xylan, acetyl glucuronoxylan from aspen, ivory nut mannan, acetylated konjac glucomannan, potato starch, heparin, hyaluronic acid, and chitosan |
? |
- |
? |
