Literature summary for 4.2.2.13 extracted from

Rozeboom, H.J.; Yu, S.; Madrid, S.; Kalk, K.H.; Zhang, R.; Dijkstra, B.W.
Crystal structure of alpha-1,4-glucan lyase, a unique glycoside hydrolase family member with a novel catalytic mechanism (2013), J. Biol. Chem., 288, 26764-26774.

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure contains a (beta/alpha)8-barrel catalytic domain with B and B' subdomains, an N-terminal domain N, and the C-terminal domains C and D. The N-terminal domain binds a trisaccharide. Complexes of the enzyme with acarbose and 1-dexoynojirimycin and two different covalent glycosyl-enzyme intermediates show that the aspartic acid residues Asp553 and Asp665 are the catalytic nucleophile and acid, respectively. The catalytic nucleophile is in a position to act also as a base that abstracts a proton from the C2 carbon atom of the covalently bound subsite -1 glucosyl residue	Gracilariopsis lemaneiformis

Crystallization (Comment)

Organism

structure contains a (beta/alpha)8-barrel catalytic domain with B and B' subdomains, an N-terminal domain N, and the C-terminal domains C and D. The N-terminal domain binds a trisaccharide. Complexes of the enzyme with acarbose and 1-dexoynojirimycin and two different covalent glycosyl-enzyme intermediates show that the aspartic acid residues Asp553 and Asp665 are the catalytic nucleophile and acid, respectively. The catalytic nucleophile is in a position to act also as a base that abstracts a proton from the C2 carbon atom of the covalently bound subsite -1 glucosyl residue

Gracilariopsis lemaneiformis

Organism

Organism	UniProt	Comment	Textmining
Gracilariopsis lemaneiformis	Q9STC1	-	-

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Release 2023.1 (January 2023)