BRENDA - Enzyme Database

In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis

O'Reilly, M.K.; Zhang, G.; Imperiali, B.; Biochemistry 45, 9593-9603 (2006) View publication on PubMed

Data extracted from this reference:

Cloned(Commentary)
EC Number
Cloned (Commentary)
Organism
2.4.1.131
overexpression in Escherichia coli. Two Alg2 constructs are expressed and isolated, one with the N-terminal TRX domain and C-terminal His and V5 epitope tags and the other with only an N-terminal His tag
Saccharomyces cerevisiae
2.4.1.132
overexpression in Escherichia coli. Two Alg2 constructs are expressed and isolated, one with the N-terminal TRX domain and C-terminal His and V5 epitope tags and the other with only an N-terminal His tag
Saccharomyces cerevisiae
2.4.1.257
overexpression in Escherichia coli. Two Alg2 constructs are expressed and isolated, one with the N-terminal TRX domain and C-terminal His and V5 epitope tags and the other with only an N-terminal His tag
Saccharomyces cerevisiae
Engineering
EC Number
Protein Variants
Commentary
Organism
2.4.1.131
E405A
mutation causes nearly complete abrogation of product formation
Saccharomyces cerevisiae
2.4.1.131
E405A/E413A
completely inactive mutant enzyme
Saccharomyces cerevisiae
2.4.1.131
E413A
activity is indistinguishable from that of the wild-type under comparable conditions
Saccharomyces cerevisiae
2.4.1.132
E335A
significant lower level of product formation
Saccharomyces cerevisiae
2.4.1.132
E335A/E343A
significant lower level of product formation, identical to that of the E335A mutant
Saccharomyces cerevisiae
2.4.1.132
E343A
no activity
Saccharomyces cerevisiae
2.4.1.257
E335A
significant lower level of product formation
Saccharomyces cerevisiae
2.4.1.257
E335A/E343A
significant lower level of product formation, identical to that of the E335A mutant
Saccharomyces cerevisiae
2.4.1.257
E343A
no activity
Saccharomyces cerevisiae
Localization
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.131
membrane
-
Saccharomyces cerevisiae
16020
-
2.4.1.132
membrane
-
Saccharomyces cerevisiae
16020
-
2.4.1.257
membrane
-
Saccharomyces cerevisiae
16020
-
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
2.4.1.131
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Saccharomyces cerevisiae
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol. Biosynthesis of asparagine-linked glycoproteins, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
-
?
2.4.1.132
GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Saccharomyces cerevisiae
the biosynthesis of asparagine-linked glycoproteins utilizes a dolichylpyrophosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol
-
-
?
2.4.1.257
GDP-alpha-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Saccharomyces cerevisiae
the biosynthesis of asparagine-linked glycoproteins utilizes a dolichylpyrophosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
-
?
Organism
EC Number
Organism
UniProt
Commentary
Textmining
2.4.1.131
Saccharomyces cerevisiae
P53954
-
-
2.4.1.132
Saccharomyces cerevisiae
P43636
-
-
2.4.1.257
Saccharomyces cerevisiae
P43636
-
-
Purification (Commentary)
EC Number
Purification (Commentary)
Organism
2.4.1.131
-
Saccharomyces cerevisiae
2.4.1.132
-
Saccharomyces cerevisiae
2.4.1.257
-
Saccharomyces cerevisiae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
2.4.1.131
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol. Biosynthesis of asparagine-linked glycoproteins, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway
707472
Saccharomyces cerevisiae
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
-
-
?
2.4.1.131
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol
707472
Saccharomyces cerevisiae
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
-
-
?
2.4.1.131
additional information
Alg11 mannosyltransferase shows no activity with Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol
707472
Saccharomyces cerevisiae
?
-
-
-
?
2.4.1.132
GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
the biosynthesis of asparagine-linked glycoproteins utilizes a dolichylpyrophosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
707472
Saccharomyces cerevisiae
GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol
-
-
-
?
2.4.1.132
GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Alg2 carries out an alpha1,3-mannosylation of Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
707472
Saccharomyces cerevisiae
GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol
-
-
-
?
2.4.1.132
additional information
Alg2 shows no activity with D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol
707472
Saccharomyces cerevisiae
?
-
-
-
?
2.4.1.257
GDP-alpha-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
the biosynthesis of asparagine-linked glycoproteins utilizes a dolichylpyrophosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
707472
Saccharomyces cerevisiae
GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
-
-
?
2.4.1.257
GDP-alpha-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
707472
Saccharomyces cerevisiae
GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
-
-
?
2.4.1.257
additional information
Alg2 shows no activity with D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol
707472
Saccharomyces cerevisiae
?
-
-
-
?
Synonyms
EC Number
Synonyms
Commentary
Organism
2.4.1.131
Alg11
-
Saccharomyces cerevisiae
2.4.1.132
Alg2
-
Saccharomyces cerevisiae
2.4.1.257
Alg2
-
Saccharomyces cerevisiae
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.4.1.131
37
-
-
Saccharomyces cerevisiae
2.4.1.132
37
-
assay at
Saccharomyces cerevisiae
2.4.1.257
37
-
assay at
Saccharomyces cerevisiae
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.4.1.131
7.2
-
-
Saccharomyces cerevisiae
2.4.1.132
7.2
-
assay at
Saccharomyces cerevisiae
2.4.1.257
7.2
-
assay at
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
2.4.1.131
overexpression in Escherichia coli. Two Alg2 constructs are expressed and isolated, one with the N-terminal TRX domain and C-terminal His and V5 epitope tags and the other with only an N-terminal His tag
Saccharomyces cerevisiae
2.4.1.132
overexpression in Escherichia coli. Two Alg2 constructs are expressed and isolated, one with the N-terminal TRX domain and C-terminal His and V5 epitope tags and the other with only an N-terminal His tag
Saccharomyces cerevisiae
2.4.1.257
overexpression in Escherichia coli. Two Alg2 constructs are expressed and isolated, one with the N-terminal TRX domain and C-terminal His and V5 epitope tags and the other with only an N-terminal His tag
Saccharomyces cerevisiae
Engineering (protein specific)
EC Number
Protein Variants
Commentary
Organism
2.4.1.131
E405A
mutation causes nearly complete abrogation of product formation
Saccharomyces cerevisiae
2.4.1.131
E405A/E413A
completely inactive mutant enzyme
Saccharomyces cerevisiae
2.4.1.131
E413A
activity is indistinguishable from that of the wild-type under comparable conditions
Saccharomyces cerevisiae
2.4.1.132
E335A
significant lower level of product formation
Saccharomyces cerevisiae
2.4.1.132
E335A/E343A
significant lower level of product formation, identical to that of the E335A mutant
Saccharomyces cerevisiae
2.4.1.132
E343A
no activity
Saccharomyces cerevisiae
2.4.1.257
E335A
significant lower level of product formation
Saccharomyces cerevisiae
2.4.1.257
E335A/E343A
significant lower level of product formation, identical to that of the E335A mutant
Saccharomyces cerevisiae
2.4.1.257
E343A
no activity
Saccharomyces cerevisiae
Localization (protein specific)
EC Number
Localization
Commentary
Organism
GeneOntology No.
Textmining
2.4.1.131
membrane
-
Saccharomyces cerevisiae
16020
-
2.4.1.132
membrane
-
Saccharomyces cerevisiae
16020
-
2.4.1.257
membrane
-
Saccharomyces cerevisiae
16020
-
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
2.4.1.131
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Saccharomyces cerevisiae
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol. Biosynthesis of asparagine-linked glycoproteins, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
-
?
2.4.1.132
GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Saccharomyces cerevisiae
the biosynthesis of asparagine-linked glycoproteins utilizes a dolichylpyrophosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol
-
-
?
2.4.1.257
GDP-alpha-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Saccharomyces cerevisiae
the biosynthesis of asparagine-linked glycoproteins utilizes a dolichylpyrophosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
2.4.1.131
-
Saccharomyces cerevisiae
2.4.1.132
-
Saccharomyces cerevisiae
2.4.1.257
-
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
2.4.1.131
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol. Biosynthesis of asparagine-linked glycoproteins, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway
707472
Saccharomyces cerevisiae
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
-
-
?
2.4.1.131
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
mannosyltransferase Alg11 carries out two consecutive alpha-1,2-mannosylation steps of the substrate Manalpha1,3-(Manalpha1,6)-Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol
707472
Saccharomyces cerevisiae
2 GDP + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
-
-
?
2.4.1.131
additional information
Alg11 mannosyltransferase shows no activity with Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol
707472
Saccharomyces cerevisiae
?
-
-
-
?
2.4.1.132
GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
the biosynthesis of asparagine-linked glycoproteins utilizes a dolichylpyrophosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
707472
Saccharomyces cerevisiae
GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol
-
-
-
?
2.4.1.132
GDP-alpha-D-mannose + D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Alg2 carries out an alpha1,3-mannosylation of Man-beta1,4-GlcNAc-beta1,4-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
707472
Saccharomyces cerevisiae
GDP + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-GlcNAc-diphosphodolichol
-
-
-
?
2.4.1.132
additional information
Alg2 shows no activity with D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol
707472
Saccharomyces cerevisiae
?
-
-
-
?
2.4.1.257
GDP-alpha-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
the biosynthesis of asparagine-linked glycoproteins utilizes a dolichylpyrophosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
707472
Saccharomyces cerevisiae
GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
-
-
?
2.4.1.257
GDP-alpha-D-mannose + D-Man-alpha-(1->3)-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
Alg2 carries out an alpha1,3-mannosylation of D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway
707472
Saccharomyces cerevisiae
GDP + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
-
-
-
?
2.4.1.257
additional information
Alg2 shows no activity with D-Man-beta-(1-4)-D-GlcNAc-beta-(1-4)-D-GlcNAc-diphosphodolichol
707472
Saccharomyces cerevisiae
?
-
-
-
?
Temperature Optimum [°C] (protein specific)
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.4.1.131
37
-
-
Saccharomyces cerevisiae
2.4.1.132
37
-
assay at
Saccharomyces cerevisiae
2.4.1.257
37
-
assay at
Saccharomyces cerevisiae
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.4.1.131
7.2
-
-
Saccharomyces cerevisiae
2.4.1.132
7.2
-
assay at
Saccharomyces cerevisiae
2.4.1.257
7.2
-
assay at
Saccharomyces cerevisiae