Cloned (Comment) | Organism |
---|---|
- |
Streptomyces coelicolor |
- |
Micromonospora aurantiaca |
Crystallization (Comment) | Organism |
---|---|
structure of the catalytic domain, residues 37-230, to 1.08 A resolution. The active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry | Streptomyces coelicolor |
structure of the catalytic domain, residues 37-230, to 1.08 A resolution. The active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry | Micromonospora aurantiaca |
Protein Variants | Comment | Organism |
---|---|---|
A148G | mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54 | Streptomyces coelicolor |
A148S | mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54 | Streptomyces coelicolor |
D140A | mutant shows moderately reduced activity and essentially unchanged oxidative regioselectivity | Micromonospora aurantiaca |
additional information | neither truncation of the LPMO10B family 2 carbohydrate-binding module nor mutations altering access to the solvent-exposed axial copper coordination site significantly change the C1:C4 oxidation ratio | Micromonospora aurantiaca |
N85F | mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.9 | Micromonospora aurantiaca |
W82Y | mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 2.0 | Micromonospora aurantiaca |
W82Y/N85F | mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 10.9 | Micromonospora aurantiaca |
W82Y/N85F/Q141W | mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.1 | Micromonospora aurantiaca |
W82Y/N85F/Y116F | mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 14.7 | Micromonospora aurantiaca |
W82Y/N85F/Y116F/Q141W | mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.8 | Micromonospora aurantiaca |
W88Y/N91F | mutation leads to loss of C4 oxidation, i.e to the activity of EC 1.14.99.54 | Streptomyces coelicolor |
Y116F | no changes in the C1:C4 oxidation ratio | Micromonospora aurantiaca |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | - |
Streptomyces coelicolor | |
Cu2+ | the active site in is formed by residues His-37 and His-144 that coordinate the copper atom in a T-shaped geometry | Micromonospora aurantiaca |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Micromonospora aurantiaca | D9SZQ3 | - |
- |
Micromonospora aurantiaca DSM 43813 | D9SZQ3 | - |
- |
Streptomyces coelicolor | Q9RJC1 | - |
- |
Streptomyces coelicolor ATCC BAA-471 | Q9RJC1 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
chitin + ascorbic acid + O2 | - |
Streptomyces coelicolor | ? + dehydroascorbate + H2O | - |
? | |
chitin + ascorbic acid + O2 | - |
Micromonospora aurantiaca | ? + dehydroascorbate + H2O | - |
? | |
chitin + ascorbic acid + O2 | - |
Streptomyces coelicolor ATCC BAA-471 | ? + dehydroascorbate + H2O | - |
? | |
chitin + ascorbic acid + O2 | - |
Micromonospora aurantiaca DSM 43813 | ? + dehydroascorbate + H2O | - |
? | |
phosphoric acid swollen cellulase + ascorbic acid + O2 | - |
Streptomyces coelicolor | ? + dehydroascorbate + H2O | - |
? | |
phosphoric acid swollen cellulase + ascorbic acid + O2 | - |
Micromonospora aurantiaca | ? + dehydroascorbate + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
chitin-binding domain 3 protein | - |
Micromonospora aurantiaca |
LPMO10B | - |
Streptomyces coelicolor |
LPMO10B | - |
Micromonospora aurantiaca |
Micau_1630 | - |
Micromonospora aurantiaca |
SCO0643 | - |
Streptomyces coelicolor |