5.4.99.11: isomaltulose synthase
This is an abbreviated version!
For detailed information about isomaltulose synthase, go to the full flat file.
Word Map on EC 5.4.99.11
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5.4.99.11
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synthesis
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erwinia
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rhapontici
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palatinose
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protaminobacter
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2.4.1.1
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pantoea
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1,4-alpha-d-glucan:orthophosphate
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molasses
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plymuthica
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food industry
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vacuole-targeted
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dispersa
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whiteflies
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bemisia
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honeydew
- 5.4.99.11
- synthesis
- erwinia
- rhapontici
- palatinose
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protaminobacter
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2.4.1.1
- pantoea
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1,4-alpha-d-glucan:orthophosphate
- molasses
- plymuthica
- food industry
-
vacuole-targeted
- dispersa
- whiteflies
- bemisia
- honeydew
Reaction
Synonyms
alpha-Glucosyltransferase, alpha-glycosyl transferase, Avin_08330, AZOG, EC 5.4.99.10, esi, isomaltulose synthase, Isomaltulose synthetase, MutB, NX-5, PalI, Pall, PdSIase, SIase, SmuA, Sucrose 6-glucosylmutase, Sucrose alpha-glucosyltransferase, sucrose isomerase, Sucrose mutase, Synthase, isomaltulose, Trehalulose synthase
ECTree
5.4.99.11 isomaltulose synthaseAdvanced search results
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results (General Information
General Information on EC 5.4.99.11 - isomaltulose synthase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
the enzyme belongs to the glycoside hydrolase family 13 (GH13) in the CAZy classification
physiological function
additional information
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
Paraburkholderia acidicola
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
Erwinia sp. D12
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
physiological function
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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physiological function
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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physiological function
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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physiological function
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
-
physiological function
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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physiological function
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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physiological function
Erwinia rhapontici wac2928
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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physiological function
Paraburkholderia acidicola MX-45
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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physiological function
Serratia plymuthica ATCC 15928
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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physiological function
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physiological functions of isomaltulose and biochemical properties of sucrose isomerases, as well as biological isomaltulose production from sucrose using sucrose isomerase, overview
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additional information
active site structure and substrate and ligand binding structures, overview
additional information
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active site structure and substrate and ligand binding structures, overview
additional information
enzyme-substrate complex, docking study with sucrose and fructose
additional information
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enzyme-substrate complex, docking study with sucrose and fructose
additional information
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structural basis for the product specificity of NX-5, docking of fructofuranose and fructopyranose into the active site of the enzyme mutant D241A-glucose complex, molecular dynamics simulations, molecular mechanism controlling sucrose isomer formation, overview. Phe297 and Phe321 in enzyme NX-5 form an aromatic clamp near the entrance of the active pocket. Residues Asp102, His145, Arg239, His368, Asp369, Glu428, and Arg456 are responsible for sucrose binding and residues Asp241 (the nucleophile) and Glu295 (the acid catalyst) are crucial for sucrose hydrolysis. The active site pocket is stabilized by the salt bridge interactions between Arg239-Asp241, Asp102-Arg456 and Asp369-Arg456. Residues Arg325 and Arg328 are located in the325RLDRD329 motif and play roles in the product specificity
additional information
proteins AS9 PalI and SmuA differ in only one amino acid, structure of the wild-type sucrose isomerases is obtained by single point mutation through pymol using the crystal structure of SmuA from Protaminobacter rubrum strain CBS 547.77 (PDB ID 3GBD). Homology models of structures of the mutant sucrose isomerases are constructed based on the crystal structure of SmuA, using the EMBL-EBI server
additional information
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proteins AS9 PalI and SmuA differ in only one amino acid, structure of the wild-type sucrose isomerases is obtained by single point mutation through pymol using the crystal structure of SmuA from Protaminobacter rubrum strain CBS 547.77 (PDB ID 3GBD). Homology models of structures of the mutant sucrose isomerases are constructed based on the crystal structure of SmuA, using the EMBL-EBI server
additional information
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the unique RLDRD motif is located in a loop adjacent to the active site cleft and is determined to play an important role in the isomerization process and in the control of product specificity
additional information
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the unique RLDRD motif is located in a loop adjacent to the active site cleft and is determined to play an important role in the isomerization process and in the control of product specificity
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additional information
-
enzyme-substrate complex, docking study with sucrose and fructose
-
additional information
-
proteins AS9 PalI and SmuA differ in only one amino acid, structure of the wild-type sucrose isomerases is obtained by single point mutation through pymol using the crystal structure of SmuA from Protaminobacter rubrum strain CBS 547.77 (PDB ID 3GBD). Homology models of structures of the mutant sucrose isomerases are constructed based on the crystal structure of SmuA, using the EMBL-EBI server
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additional information
Serratia plymuthica ATCC 15928
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the unique RLDRD motif is located in a loop adjacent to the active site cleft and is determined to play an important role in the isomerization process and in the control of product specificity
-
additional information
-
structural basis for the product specificity of NX-5, docking of fructofuranose and fructopyranose into the active site of the enzyme mutant D241A-glucose complex, molecular dynamics simulations, molecular mechanism controlling sucrose isomer formation, overview. Phe297 and Phe321 in enzyme NX-5 form an aromatic clamp near the entrance of the active pocket. Residues Asp102, His145, Arg239, His368, Asp369, Glu428, and Arg456 are responsible for sucrose binding and residues Asp241 (the nucleophile) and Glu295 (the acid catalyst) are crucial for sucrose hydrolysis. The active site pocket is stabilized by the salt bridge interactions between Arg239-Asp241, Asp102-Arg456 and Asp369-Arg456. Residues Arg325 and Arg328 are located in the325RLDRD329 motif and play roles in the product specificity
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