Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.99.53 extracted from

  • Forsberg, Z.; Bissaro, B.; Gullesen, J.; Dalhus, B.; Vaaje-Kolstad, G.; Eijsink, V.G.H.
    Structural determinants of bacterial lytic polysaccharide monooxygenase functionality (2018), J. Biol. Chem., 293, 1397-1412.
    View publication on PubMed
Search for more literature for 1.14.99.53

Cloned(Commentary)

Cloned (Comment) Organism
-
 Micromonospora aurantiaca (nom. illeg.)
-
 Streptomyces coelicolor

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of the catalytic domain (residues 37-230, lacking the linker and the CBM2) to 1.08 A resolution. Structure shows the typical LPMO fold with a central beta-sandwich made up by two distorted beta-sheets connected by several loops and helices. The active site is formed by His37 and His144 that coordinate the copper atom in a T-shaped geometry Micromonospora aurantiaca (nom. illeg.)
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 (nom. illeg.)
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

Protein Variants

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 (nom. illeg.)
additional information neither truncation of theLPMO10B 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 (nom. illeg.)
N85F mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.9 Micromonospora aurantiaca (nom. illeg.)
W82Y mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 2.0 Micromonospora aurantiaca (nom. illeg.)
W82Y/N85F mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 10.9 Micromonospora aurantiaca (nom. illeg.)
W82Y/N85F/Q141W mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.1 Micromonospora aurantiaca (nom. illeg.)
W82Y/N85F/Q141W loss of chitin monooxygenase activity, 12.21% residual cellulose C1- and 2.1% residual C4-oxidizing activity, ratio C1:C4-activity is 5.06 Micromonospora aurantiaca (nom. illeg.)
W82Y/N85F/Y116F mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 14.7 Micromonospora aurantiaca (nom. illeg.)
W82Y/N85F/Y116F/Q141W mutation changes the C1:C4 oxidation ratio from 0.9 (for the wild-type) to 5.8 Micromonospora aurantiaca (nom. illeg.)
W82Y/N85F/Y116F/Q141W loss of chitin oxidizinbg activity, 10.2% residual cellulose C1- and 1.6% residual C4-oxidizing activity, ratio C1:C4-activity is 5.78 Micromonospora aurantiaca (nom. illeg.)
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 (nom. illeg.)

Metals/Ions

Metals/Ions Comment Organism Structure
copper the active site is formed by His37 and His144 that coordinate the copper atom in a T-shaped geometry Micromonospora aurantiaca (nom. illeg.)
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 (nom. illeg.)
Cu2+
-
 Streptomyces coelicolor

Organism

Organism UniProt Comment Textmining
Micromonospora aurantiaca (nom. illeg.) D9SZQ3
-
-
Micromonospora aurantiaca (nom. illeg.) D9SZQ3 cf. EC 1.14.99.56, 1.14.99.54
-
Micromonospora aurantiaca (nom. illeg.) DSM 43813 D9SZQ3
-
-
Micromonospora aurantiaca (nom. illeg.) DSM 43813 D9SZQ3 cf. EC 1.14.99.56, 1.14.99.54
-
Streptomyces coelicolor Q9RJC1
-
-
Streptomyces coelicolor ATCC BAA-471 Q9RJC1
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
chitin + ascorbic acid + O2
-
 Micromonospora aurantiaca (nom. illeg.) ? + dehydroascorbate + H2O
-
 ?
chitin + ascorbic acid + O2
-
 Streptomyces coelicolor ? + dehydroascorbate + H2O
-
 ?
chitin + ascorbic acid + O2
-
 Streptomyces coelicolor ATCC BAA-471 ? + dehydroascorbate + H2O
-
 ?
chitin + ascorbic acid + O2
-
 Micromonospora aurantiaca (nom. illeg.) DSM 43813 ? + dehydroascorbate + H2O
-
 ?
phosphoric acid swollen cellulase + ascorbic acid + O2
-
 Micromonospora aurantiaca (nom. illeg.) ? + dehydroascorbate + H2O
-
 ?
phosphoric acid swollen cellulase + ascorbic acid + O2
-
 Streptomyces coelicolor ? + dehydroascorbate + H2O
-
 ?
phosphoric acid swollen cellulase + ascorbic acid + O2
-
 Streptomyces coelicolor ATCC BAA-471 ? + dehydroascorbate + H2O
-
 ?
phosphoric acid swollen cellulase + ascorbic acid + O2
-
 Micromonospora aurantiaca (nom. illeg.) DSM 43813 ? + dehydroascorbate + H2O
-
 ?

Synonyms

Synonyms Comment Organism
chitin-binding domain 3 protein
-
 Micromonospora aurantiaca (nom. illeg.)
LPMO10B
-
 Micromonospora aurantiaca (nom. illeg.)
LPMO10B
-
 Streptomyces coelicolor
Micau_1630
-
 Micromonospora aurantiaca (nom. illeg.)
SCO0643
-
 Streptomyces coelicolor