Literature summary for 3.2.1.131 extracted from

Xue, Y.; Yu, J.; Song, X.; Peng, J.; Shao, W.
Over-expression of xylanolytic alpha-glucuronidase from Thermotoga maritima in the pHsh system of Escherichia coli for the production of xylobiose from xylan (2008), Afr. J. Biotechnol., 7, 2454-2461 .

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Application

Application	Comment	Organism
synthesis	application in enzymatic production of xylooligosaccharides from xylan. The high level of the thermostable alpha-glucuronidase from Thermotoga maritima, combined purification by a simple heat treament, has a considerable potential in the production of xylooligosaccharide, especially xylobiose	Thermotoga maritima

Cloned(Commentary)

Cloned (Comment)	Organism
expression of the gene in Escherichia coli is very low, even in an expression plasmid construct with optimized transcription and translation start sequences. Rare codons for arginine (AGA and AGG) and isoleucine (AUA) affect the AguA from Thermothoga maritima in Escherichia coli. x03In order to raise gene expression to meet industrial requirements, the rare codons in the N-terminal region of the AguA from Thermotoga maritima are replaced, and the aguA gene is overexpressed using the heat-inducible vector pHsh. The application of the recombinant enzyme in the production of xylobioses from xylan is also described	Thermotoga maritima

Cloned (Comment)

Organism

expression of the gene in Escherichia coli is very low, even in an expression plasmid construct with optimized transcription and translation start sequences. Rare codons for arginine (AGA and AGG) and isoleucine (AUA) affect the AguA from Thermothoga maritima in Escherichia coli. x03In order to raise gene expression to meet industrial requirements, the rare codons in the N-terminal region of the AguA from Thermotoga maritima are replaced, and the aguA gene is overexpressed using the heat-inducible vector pHsh. The application of the recombinant enzyme in the production of xylobioses from xylan is also described

Thermotoga maritima

Organism

Organism	UniProt	Comment	Textmining
Thermotoga maritima	P96105	-	-
Thermotoga maritima DSM 3109	P96105	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
4-O-methyl-D-glucuronoxylan + H2O	the enzyme is able to remove 4-O-methylglucuronic acid groups from 4-O-methyl-D-glucuronoxylan	Thermotoga maritima	4-O-methyl-alpha-D-glucuronic acid + ?	-	?
4-O-methyl-D-glucuronoxylan + H2O	the enzyme is able to remove 4-O-methylglucuronic acid groups from 4-O-methyl-D-glucuronoxylan	Thermotoga maritima DSM 3109	4-O-methyl-alpha-D-glucuronic acid + ?	-	?
birchwood xylan + H2O	the enzyme is able to remove 4-O-methylglucuronic acid groups from birchwood xylan	Thermotoga maritima	4-O-methyl-alpha-D-glucuronic acid + ?	-	?
birchwood xylan + H2O	the enzyme is able to remove 4-O-methylglucuronic acid groups from birchwood xylan	Thermotoga maritima DSM 3109	4-O-methyl-alpha-D-glucuronic acid + ?	-	?
oat spelt xylan + H2O	the enzyme is able to remove 4-O-methylglucuronic acid groups from birchwood xylan	Thermotoga maritima	4-O-methyl-alpha-D-glucuronic acid + ?	-	?
oat spelt xylan + H2O	the enzyme is able to remove 4-O-methylglucuronic acid groups from birchwood xylan	Thermotoga maritima DSM 3109	4-O-methyl-alpha-D-glucuronic acid + ?	-	?

Synonyms

Synonyms	Comment	Organism
AguA	-	Thermotoga maritima
xylanolytic alpha-glucuronidase	-	Thermotoga maritima

General Information

General Information	Comment	Organism
metabolism	one of the rate-limiting enzymes for the degradation of xylan	Thermotoga maritima