Literature summary for 5.1.3.8 extracted from

Klermund, L.; Riederer, A.; Groher, A.; Castiglione, K.
High-level soluble expression of a bacterial N-acyl-D-glucosamine 2-epimerase in recombinant Escherichia coli (2015), Protein Expr. Purif., 111, 36-41 .

Cloned(Commentary)

Cloned (Comment)	Organism
gene age, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) at 37°C with coexpression of chaperones GroEL/GroES, 264fold increased AGE activity and maximum yield of 22.5 mg isolated AvaAGE per liter shake flask culture, compared to the starting conditions, method optimization, enhancement of soluble expression via chaperones, temperature dependence of soluble expression, and enhancement of soluble expression via fusion tags, overview	Trichormus variabilis

Cloned (Comment)

Organism

gene age, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) at 37°C with coexpression of chaperones GroEL/GroES, 264fold increased AGE activity and maximum yield of 22.5 mg isolated AvaAGE per liter shake flask culture, compared to the starting conditions, method optimization, enhancement of soluble expression via chaperones, temperature dependence of soluble expression, and enhancement of soluble expression via fusion tags, overview

Trichormus variabilis

Protein Variants

Protein Variants	Comment	Organism
additional information	the majority of biocatalytic approaches for Neu5Ac synthesis involve an N-acylglucosamine 2-epimerase (AGE, EC 5.3.1.8) in combination with an N-acetylneuraminate lyase (NAL, EC 4.1.3.3)	Trichormus variabilis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
N-Acyl-D-glucosamine	Trichormus variabilis	-	N-Acyl-D-mannosamine	-	r

Organism

Organism	UniProt	Comment	Textmining
Trichormus variabilis	Q3M763	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)	Trichormus variabilis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-Acyl-D-glucosamine	-	Trichormus variabilis	N-Acyl-D-mannosamine	-	r

Synonyms

Synonyms	Comment	Organism
AGE	-	Trichormus variabilis
AvaAGE	-	Trichormus variabilis
N-acyl-D-glucosamine 2-epimerase	-	Trichormus variabilis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Trichormus variabilis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Trichormus variabilis

General Information

General Information	Comment	Organism
additional information	the majority of biocatalytic approaches for Neu5Ac synthesis involve an N-acylglucosamine 2-epimerase (AGE, EC 5.3.1.8) in combination with an N-acetylneuraminate lyase (NAL, EC 4.1.3.3)	Trichormus variabilis
physiological function	N-acyl-D-glucosamine 2-epimerase (AGE) is an important enzyme for the biocatalytic synthesis of N-acetylneuraminic acid (Neu5Ac)	Trichormus variabilis