Literature summary for 4.2.2.8 extracted from

Dong, W.; Lu, W.; McKeehan, W.L.; Luo, Y.; Ye, S.
Structural basis of heparan sulfate-specific degradation by heparinase III (2012), Protein Cell, 3, 950-961.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacteroides thetaiotaomicron

Crystallization (Commentary)

Crystallization (Comment)	Organism
isoform HepIII, to 1.6 A resolution. The overall architecture of HepIII belongs to the (alpha/alpha)5 toroid subclass with an N-terminal toroid-like domain and a C-terminal beta-sandwich domain. An elimination mechanism is suggested whereby Asn260 and His464 neutralize the carboxylic group, whereas Tyr314 serves both as a general base in C-5 proton abstraction, and a general acid in a proton donation to reconstitute the terminal hydroxyl group, respectively	Bacteroides thetaiotaomicron

Crystallization (Comment)

Organism

isoform HepIII, to 1.6 A resolution. The overall architecture of HepIII belongs to the (alpha/alpha)5 toroid subclass with an N-terminal toroid-like domain and a C-terminal beta-sandwich domain. An elimination mechanism is suggested whereby Asn260 and His464 neutralize the carboxylic group, whereas Tyr314 serves both as a general base in C-5 proton abstraction, and a general acid in a proton donation to reconstitute the terminal hydroxyl group, respectively

Bacteroides thetaiotaomicron

Organism

Organism	UniProt	Comment	Textmining
Bacteroides thetaiotaomicron	Q89YR9	-	-
Bacteroides thetaiotaomicron DSM 2079	Q89YR9	-	-

Synonyms

Synonyms	Comment	Organism
HepIII	-	Bacteroides thetaiotaomicron

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Release 2023.1 (January 2023)