| Cloned (Comment) | Organism |
|---|---|
| codon-optimized expression in Escherichia coli | Jonesia denitrificans |
| Crystallization (Comment) | Organism |
|---|---|
| 1.55 A resolution structure of N-terminal LPMO10A module reveals deletions of interacting loops that protrude from the core beta-sandwich scaffold in larger LPMO10s | Jonesia denitrificans |
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 15500 | - |
- |
Jonesia denitrificans |
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Jonesia denitrificans | C7R4I0 | protein comprises a small N-terminal LPMO10 module named LPMO10A followed by a family 5/12 CBM and a C-terminal GH18 module | - |
| Jonesia denitrificans DSM 20603 | C7R4I0 | protein comprises a small N-terminal LPMO10 module named LPMO10A followed by a family 5/12 CBM and a C-terminal GH18 module | - |
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| alpha-chitin + ascorbate + O2 | - |
Jonesia denitrificans | C1-oxidized chitooligosaccharides + dehydroascorbate + H2O | products are C1-oxidized chitooligomers, mainly tetramers and hexamers | ? | |
| alpha-chitin + ascorbate + O2 | - |
Jonesia denitrificans DSM 20603 | C1-oxidized chitooligosaccharides + dehydroascorbate + H2O | products are C1-oxidized chitooligomers, mainly tetramers and hexamers | ? | |
| beta-chitin + ascorbate + O2 | beta-chitin is preferred over alpha-chitin | Jonesia denitrificans | C1-oxidized chitooligosaccharides + dehydroascorbate + H2O | products are C1-oxidized chitooligomers, mainly tetramers and hexamers | ? | |
| beta-chitin + ascorbate + O2 | beta-chitin is preferred over alpha-chitin | Jonesia denitrificans DSM 20603 | C1-oxidized chitooligosaccharides + dehydroascorbate + H2O | products are C1-oxidized chitooligomers, mainly tetramers and hexamers | ? | |
| additional information | the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved | Jonesia denitrificans | ? | - |
? | |
| additional information | the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved | Jonesia denitrificans DSM 20603 | ? | - |
? |
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 15500, N-terminal LPMO10A module | Jonesia denitrificans |
| Synonyms | Comment | Organism |
|---|---|---|
| Jden_1381 | - |
Jonesia denitrificans |
| LPMO10A | - |
Jonesia denitrificans |