2.4.1.4: amylosucrase
This is an abbreviated version!
For detailed information about amylosucrase, go to the full flat file.
Word Map on EC 2.4.1.4
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2.4.1.4
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neisseria
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polysaccharea
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deinococcus
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geothermalis
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synthesis
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food industry
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biotechnology
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amylose-like
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transglucosylation
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waxy
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drug development
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turanose
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asases
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transglucosidase
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amylopectin
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c-myc-binding
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maltooligosaccharides
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glycoside-hydrolase
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trehalulose
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industry
- 2.4.1.4
- neisseria
- polysaccharea
-
deinococcus
- geothermalis
- synthesis
- food industry
- biotechnology
-
amylose-like
-
transglucosylation
-
waxy
- drug development
- turanose
- asases
- transglucosidase
- amylopectin
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c-myc-binding
- maltooligosaccharides
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glycoside-hydrolase
- trehalulose
- industry
Reaction
Synonyms
AaAS, ACAS, AmAS, AMS, Amy-1, ASASE, BtAS, CcAS, DGAS, DRAS, DRpAS, glucosyltransferase, sucrose-1,4-alpha-glucan, MaAS, MFAS, More, NPAS, NsAS, sucrose-glucan glucosyltransferase, SyAS
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General Information
General Information on EC 2.4.1.4 - amylosucrase
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evolution
physiological function
additional information
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amylosucrase belongs to the glycoside hydrolase family 13, GH 13
evolution
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amylosucrase is a kind of glucosyltransferases belonging to the glycoside hydrolase family 13
evolution
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the enzyme belongs to the glycohydrolase family 13, GH13
evolution
the enzyme belongs to the glycohydrolase family 13, GH13
evolution
amylosucrase from Neisseria polysaccharea is a transglucosidase from the GH13 family of glycoside-hydrolases. Natural molecular evolution has modeled a dense hydrogen bond network at subsite 21 responsible for the specific recognition of sucrose and conversely, it has loosened interactions at the subsite 11 creating a highly promiscuous subsite 11. The residues forming these subsites are considered to be likely involved in the activity as well as the overall stability of the enzyme
evolution
the enzyme belongs to the aglycoside-hydrolase family 13. Genes spsA,sppA, frkA and amsA are grouped in a transcriptional unit that is named Suc cluster
evolution
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the enzyme belongs to the GH13 family. Amylosucrases adopt a deep pocket topology of about 15 A with the catalytic triad located at the bottom
evolution
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the enzyme belongs to the glycoside hydrolase family GH13
evolution
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the enzyme is a glucosyltransferase of the glycoside hydrolase 13 family, that does not require a nucleotide-activated sugar as a glucosyl-donor
evolution
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the putative MFAS protein shares not only catalytic residues, but also five consensus regions (CR I-V), with other ASases, although the overall protein shows a low level of amino acid sequence homology when compared with known ASases (ACAS, AMAS, DGAS, DRAS, and NPAS), overview
evolution
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the putative MFAS protein shares not only catalytic residues, but also five consensus regions (CR I-V), with other ASases, although the overall protein shows a low level of amino acid sequence homology when compared with known ASases (ACAS, AMAS, DGAS, DRAS, and NPAS), overview
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evolution
Pseudarthrobacter chlorophenolicus A6 / DSM 12829
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amylosucrase belongs to the glycoside hydrolase family 13, GH 13
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evolution
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the enzyme is a glucosyltransferase of the glycoside hydrolase 13 family, that does not require a nucleotide-activated sugar as a glucosyl-donor
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amylosucrases are sucrose-utilizing alpha-transglucosidases that naturally catalyze the synthesis of alpha-glucans, linked exclusively through alpha-1,4-linkages. Side products and in particular sucrose isomers such as turanose and trehalulose are also produced by these enzymes
physiological function
amylosucrases are sucrose-utilizing alpha-transglucosidases that naturally catalyze the synthesis of alpha-glucans, linked exclusively through alpha-1,4-linkages. Side products and in particular sucrose isomers such as turanose and trehalulose are also produced by these enzymes
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dynamics and unfolding properties of the enzyme by the gauss network model and the anisotropic network model, overview
additional information
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the catalytic domain A of DgAS adopts the typical (alpha/alpha)8-barrel of the GH family 13
additional information
the catalytic domain A of NpAS adopts the typical (alpha/alpha)8-barrel of the GH family 13
additional information
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the catalytic domain A of NpAS adopts the typical (alpha/alpha)8-barrel of the GH family 13
additional information
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active site topology and structure coparisons, overview
additional information
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Arg226, was proposed from molecular modeling studies to play an important role in the formation of the active site topology and in the accessibility of ligands to the catalytic site
additional information
essential role of enzyme subsite -1 for protein fitness and robustness
additional information
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essential role of enzyme subsite -1 for protein fitness and robustness
additional information
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ligand binding causes extensive changes in active-site topology
additional information
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loops 3, 4, and 7 of AS form an active-site pocket and play an important role in transglycosylation activity
additional information
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loops 3, 4, and 7 of AS form an active-site pocket and play an important role in transglycosylation activity
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