Literature summary for 4.2.2.7 extracted from

Xu, S.; Qiu, M.; Zhang, X.; Chen, J.
Expression and characterization of an enhanced recombinant heparinase I with chitin binding domain (2017), Int. J. Biol. Macromol., 105, 1250-1258 .

Search for more literature for 4.2.2.7

Application

Application	Comment	Organism
synthesis	expression of HepI with the chitin binding domain of Bacillus circulans chitinase A1 as a chitin-affinity tag, and the small ubiquitin-like modifier (SUMO) linker as a solvation enhancer in different fusion sequence. The constructs chitin binding domain-HepI, chitin binding domain-SUMO-HepI, SUMO-chitin binding domain-HepI and chitin binding domain-HepI-SUMO show specific enzyme activities of 1.88, 3.69, 3.44, and 2.73 IU/mg total proteins, respectively, with unfractionated heparin as substrate. Chitin binding domain-SUMO-HepI exhibits the maximum half-life (48 min) at 30°C and best thermostability under 15-50°C. All the fusion enzymes show broad pH-stability in the range of 5.4-9.0	Pedobacter heparinus

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pedobacter heparinus

Organism

Organism	UniProt	Comment	Textmining
Pedobacter heparinus	B3U3D9	-	-

Synonyms

Synonyms	Comment	Organism
HepI	-	Pedobacter heparinus

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Release 2023.1 (January 2023)