Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Jung, J.H.; Kim, M.J.; Jeong, W.S.; Seo, D.H.; Ha, S.J.; Kim, Y.W.; Park, C.S.
    Characterization of divergent pseudo-sucrose isomerase from Azotobacter vinelandii Deciphering the absence of sucrose isomerase activity (2017), Biochem. Biophys. Res. Commun., 483, 115-121 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.4.99.11 gene Avin_08330, sequence comparisons and phylogenetic tree, recombinant expression of wild-type AZOG enzyme and chimeric mutants AZF3 and AZF5 in Escherichia coli strain BL21(DE3) Azotobacter vinelandii
5.4.99.11 gene esi, sequence comparisons and phylogenetic tree, recombinant expression chimeric mutants AZF3 and AZF5 in Escherichia coli strain BL21(DE3) Enterobacter sp. FMB-1

Protein Variants

EC Number Protein Variants Comment Organism
5.4.99.11 additional information construction of chimeric mutant enzymes AZF3 and AZF5 from sucrose isomerase AZOG of Azotobacter vinelanddii and and sucrose isomerase, encoded by esi gene, from Enterobacter sp. FMB-1. Mutant AZF3 has the N-terminal region of Enterobacter SIase and C-terminal region of AZOG, while mutant AZF5 contains the N-terminal region of AZOG and C-terminal region of Enterobacter SIase. Determination of transglycosylation activity, overview. Mutant AZF3 shows altered substrate specificity and reduced activity compared to the wild-type enzyme Azotobacter vinelandii
5.4.99.11 additional information construction of chimeric mutant enzymes AZF3 and AZF5 from sucrose isomerase SIase from Enterobacter sp. strain FMB-1 and AZOG of Azotobacter vinelanddii. Mutant AZF3 has the N-terminal region of Enterobacter SIase and C-terminal region of AZOG, while mutant AZF5 contains the N-terminal region of AZOG and C-terminal region of Bacillus halodurans SIase. Gene Avin_08330 encodes the putative sucrose isomerase AZOG in the nitrogen-fixing bacterium Azotobacter vinelandii. The enzyme is a type of pseudo-sucrose isomerase harboring the RLDRD motif, a sucrose isomerase-specific region in 329-333. Neither sucrose isomerization nor hydrolysis activities are observed in recombinant AZOG. Determination of transglycosylation activity, overview. Mutant AZF3 shows altered substrate specificity and reduced activity compared to the wild-type enzyme AZOG. The sucrose is converted into isomaltose, isomatulose and trehalulose, as well as the hydrolysis products glucose and fructose by mutant AZF3, while wild-type AZOG only produces glucose and fructose Enterobacter sp. FMB-1

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.4.99.11 sucrose Enterobacter sp. FMB-1
-
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
r
5.4.99.11 sucrose Azotobacter vinelandii
-
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
r
5.4.99.11 sucrose Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137
-
6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
r

Organism

EC Number Organism UniProt Comment Textmining
5.4.99.11 Azotobacter vinelandii C1DMP8
-
-
5.4.99.11 Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137 C1DMP8
-
-
5.4.99.11 Enterobacter sp. FMB-1 B5ABD8
-
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
5.4.99.11 0.04
-
recombinant mutant AZF3, pH 6.0, 35°C, substrate isomaltulose Enterobacter sp. FMB-1
5.4.99.11 0.04
-
recombinant mutant AZF3, pH 6.0, 35°C, substrate isomaltulose Azotobacter vinelandii
5.4.99.11 0.06
-
recombinant mutant AZF3, pH 6.0, 35°C, substrate turanose Enterobacter sp. FMB-1
5.4.99.11 0.06
-
recombinant mutant AZF3, pH 6.0, 35°C, substrate turanose Azotobacter vinelandii
5.4.99.11 0.11
-
recombinant enzyme, pH 6.0, 35°C, substrate sucrose Azotobacter vinelandii
5.4.99.11 0.22
-
recombinant mutant AZF3, pH 6.0, 35°C, substrate sucrose Enterobacter sp. FMB-1
5.4.99.11 0.22
-
recombinant mutant AZF3, pH 6.0, 35°C, substrate sucrose Azotobacter vinelandii
5.4.99.11 0.52
-
recombinant enzyme, pH 6.0, 35°C, substrate kojibiose Azotobacter vinelandii
5.4.99.11 0.6
-
recombinant enzyme, pH 6.0, 35°C, substrate isomaltotriose Azotobacter vinelandii
5.4.99.11 0.97
-
recombinant enzyme, pH 6.0, 35°C, substrate methyl alpha-D-glucoside Azotobacter vinelandii
5.4.99.11 0.98
-
recombinant enzyme, pH 6.0, 35°C, substrate isomaltose Azotobacter vinelandii
5.4.99.11 1.03
-
recombinant mutant AZF3, pH 6.0, 35°C, substrate 4-nitrophenyl alpha-D-trehalose Enterobacter sp. FMB-1
5.4.99.11 1.03
-
recombinant mutant AZF3, pH 6.0, 35°C, substrate 4-nitrophenyl-alpha-D-trehalose Azotobacter vinelandii
5.4.99.11 2.33
-
recombinant enzyme, pH 6.0, 35°C, substrate isomaltulose Azotobacter vinelandii
5.4.99.11 2.9
-
recombinant enzyme, pH 6.0, 35°C, substrate 4-nitrophenyl alpha-D-trehalose Azotobacter vinelandii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.4.99.11 4-nitrophenyl alpha-D-glucoside enzyme chimeric mutant AZF3 Enterobacter sp. FMB-1 ?
-
?
5.4.99.11 4-nitrophenyl alpha-D-glucoside wild-type AZOG and enzyme chimeric mutant AZF3 Azotobacter vinelandii ?
-
?
5.4.99.11 4-nitrophenyl alpha-D-glucoside wild-type AZOG and enzyme chimeric mutant AZF3 Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137 ?
-
?
5.4.99.11 isomaltotriose wild-type AZOG Azotobacter vinelandii ?
-
?
5.4.99.11 isomaltulose enzyme chimeric mutant AZF3 Enterobacter sp. FMB-1 sucrose
-
r
5.4.99.11 isomaltulose wild-type AZOG and enzyme chimeric mutant AZF3 Azotobacter vinelandii sucrose
-
r
5.4.99.11 kojibiose wild-type AZOG Azotobacter vinelandii ?
-
?
5.4.99.11 kojibiose wild-type AZOG Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137 ?
-
?
5.4.99.11 methyl alpha-D-glucoside wild-type AZOG Azotobacter vinelandii ?
-
?
5.4.99.11 additional information enzyme substrate specificity, overview. No activity with methyl alpha-D-glucoside, trehalose, nigerose, maltose, isomaltotriose, and panose, and poor activity with kojibiose and isomaltose. The sucrose is converted into isomaltose, isomatulose and trehalulose, as well as the hydrolysis products glucose and fructose by enzyme mutant AZF3, while wild-type AZOG only produces glucose and fructose Enterobacter sp. FMB-1 ?
-
?
5.4.99.11 additional information gene Avin_08330 encodes the putative sucrose isomerase AZOG in the nitrogen-fixing bacterium Azotobacter vinelandii. The enzyme is a type of pseudo-sucrose isomerase harboring the RLDRD motif, a sucrose isomerase-specific region in 329-333. Neither sucrose isomerization nor hydrolysis activities are observed in recombinant AZOG (rAZOG). The rAZOG shows similar substrate specificity to the enzyme from Bacillus sp. O16G as it catalyzes the hydrolysis of isomaltulose and isomaltose, which contain alpha-1,6-glycosidic linkages. rAZOG generates isomaltose from the small substrate methyl-alpha-glucoside (MaG) via intermolecular transglycosylation. In addition, sucrose isomers isomaltulose and trehalulose are produced when 250 mM fructose is added to the MaG reaction mixture. Enzyme substrate specificity, overview. No activity with trehalose, maltose, nigerose, turanose, and panose. Comparison of substrate specificity with oligo-1,6-glucosidase, EC 3.2.1.10, from Bacillus halodurans strain O16G, UniProt ID BH2903, gene BH2903 Azotobacter vinelandii ?
-
?
5.4.99.11 additional information gene Avin_08330 encodes the putative sucrose isomerase AZOG in the nitrogen-fixing bacterium Azotobacter vinelandii. The enzyme is a type of pseudo-sucrose isomerase harboring the RLDRD motif, a sucrose isomerase-specific region in 329-333. Neither sucrose isomerization nor hydrolysis activities are observed in recombinant AZOG (rAZOG). The rAZOG shows similar substrate specificity to the enzyme from Bacillus sp. O16G as it catalyzes the hydrolysis of isomaltulose and isomaltose, which contain alpha-1,6-glycosidic linkages. rAZOG generates isomaltose from the small substrate methyl-alpha-glucoside (MaG) via intermolecular transglycosylation. In addition, sucrose isomers isomaltulose and trehalulose are produced when 250 mM fructose is added to the MaG reaction mixture. Enzyme substrate specificity, overview. No activity with trehalose, maltose, nigerose, turanose, and panose. Comparison of substrate specificity with oligo-1,6-glucosidase, EC 3.2.1.10, from Bacillus halodurans strain O16G, UniProt ID BH2903, gene BH2903 Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137 ?
-
?
5.4.99.11 sucrose
-
Enterobacter sp. FMB-1 6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
r
5.4.99.11 sucrose
-
Azotobacter vinelandii 6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
r
5.4.99.11 sucrose enzyme chimeric mutant AZF3 Enterobacter sp. FMB-1 6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
r
5.4.99.11 sucrose wild-type AZOG and enzyme chimeric mutant AZF3 Azotobacter vinelandii 6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
r
5.4.99.11 sucrose
-
Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137 6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
r
5.4.99.11 sucrose wild-type AZOG and enzyme chimeric mutant AZF3 Azotobacter vinelandii DJ / ATCC BAA-1303 / KCTC 12137 6-O-alpha-D-Glucopyranosyl-D-fructofuranose
-
r
5.4.99.11 turanose enzyme chimeric mutant AZF3 Enterobacter sp. FMB-1 ?
-
?
5.4.99.11 turanose enzyme chimeric mutant AZF3 Azotobacter vinelandii ?
-
?

Synonyms

EC Number Synonyms Comment Organism
5.4.99.11 Avin_08330
-
Azotobacter vinelandii
5.4.99.11 AZOG
-
Azotobacter vinelandii
5.4.99.11 esi
-
Enterobacter sp. FMB-1
5.4.99.11 Pall
-
Enterobacter sp. FMB-1
5.4.99.11 SIase
-
Enterobacter sp. FMB-1
5.4.99.11 SIase
-
Azotobacter vinelandii
5.4.99.11 sucrose isomerase
-
Enterobacter sp. FMB-1
5.4.99.11 sucrose isomerase
-
Azotobacter vinelandii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.4.99.11 30 35 assay at Azotobacter vinelandii
5.4.99.11 35
-
assay at Enterobacter sp. FMB-1

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4.99.11 6
-
assay at Enterobacter sp. FMB-1
5.4.99.11 6
-
assay at Azotobacter vinelandii