Literature summary for 4.2.2.13 extracted from

Su, H.; Dong, L.; Liu, Y.
A QM/MM study of the catalytic mechanism of alpha-1,4-glucan lyase from the red seaweed Gracilariopsis lemaneiformis (2014), RSC Adv., 4, 54398 .

No PubMed abstract available

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Organism

Organism	UniProt	Comment	Textmining
Gracilariopsis lemaneiformis	Q9STC1	-	-

Synonyms

Synonyms	Comment	Organism
Ag111	-	Gracilariopsis lemaneiformis
alpha-1,4-glucan lyase isozyme 1	-	Gracilariopsis lemaneiformis

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Release 2023.1 (January 2023)