EC Number | Crystallization (Comment) | Organism |
---|---|---|
4.2.2.13 | quantum mechanics/molecular mechanics study on mechanism. Residue D665 acts as an acid to protonate the glycoside oxygen, which is concerted with the cleavage of the glycoside bond. Residue D553 functions as the nucleophile to attack the anomeric carbon to form the glycosyl-enzyme intermediate. The glycosylation process follows a stepwise mechanism. The deprotonated residue D553 further acts as a catalytic base to abstract the C2-proton of the glucosyl residue. The proton abstraction in the deglycosylation/elimination step is calculated to be the rate-limiting step of the whole catalytic reaction | Gracilariopsis lemaneiformis |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.2.2.13 | Gracilariopsis lemaneiformis | Q9STC1 | - |
- |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.2.2.13 | Ag111 | - |
Gracilariopsis lemaneiformis |
4.2.2.13 | alpha-1,4-glucan lyase isozyme 1 | - |
Gracilariopsis lemaneiformis |