Literature summary for 3.2.1.18 extracted from

Christensen, S.; Egebjerg, J.
Cloning, expression and characterization of a sialidase gene from Arthrobacter ureafaciens (2005), Biotechnol. Appl. Biochem., 41, 225-231.

Application

Application	Comment	Organism
molecular biology	use of the enzyme in the desialylation of human recombinant erythropoietin	Paenarthrobacter ureafaciens

Cloned(Commentary)

Cloned (Comment)	Organism
expression cloning strategy to isolate the sialidase. The clone encodes a 990-amino-acid 104 kDa open-reading-frame protein containing three domains: an N-terminal catalytic domain, a linker domain with an immunoglobulin-like fold and a C-terminal domain of unknown function. Expression in Escherichia coli indicates that the sialidase promoter is active in Escherichia coli. Overexpression in Escherichia coli resulted in several truncated forms. 54 kDa truncated variant is generated, expressed and purified	Paenarthrobacter ureafaciens

Cloned (Comment)

Organism

expression cloning strategy to isolate the sialidase. The clone encodes a 990-amino-acid 104 kDa open-reading-frame protein containing three domains: an N-terminal catalytic domain, a linker domain with an immunoglobulin-like fold and a C-terminal domain of unknown function. Expression in Escherichia coli indicates that the sialidase promoter is active in Escherichia coli. Overexpression in Escherichia coli resulted in several truncated forms. 54 kDa truncated variant is generated, expressed and purified

Paenarthrobacter ureafaciens

Organism

Organism	UniProt	Comment	Textmining
Paenarthrobacter ureafaciens	Q5W7Q2	-	-

Purification (Commentary)

Purification (Comment)	Organism
54 kDa truncated histidine-tagged variant	Paenarthrobacter ureafaciens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)