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
-
c-myc-binding
- maltooligosaccharides
-
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
ECTree
2.4.1.4 amylosucraseAdvanced search results
results (
results (Subunits
Subunits on EC 2.4.1.4 - amylosucrase
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SUBUNIT 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
homodimer
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three-dimensional structure and dimer interface analysis. The quaternary organization is likely to participate in the enhanced thermal stability of the protein. Structure comparison with the amylosucrase from Neisseria polysaccharea, overview
homotetramer
monomer
additional information
?
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x * 73214, sequence calculation, x * 73000, recombinant detagged enzyme, SDS-PAGE
?
x * 72466, sequence calculation, excluding the transit peptide, x * 85000, about, recombinant SBD-fusion enzyme, SDS-PAGE
dimer
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2 * 72000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 72822, sequence calculation
dimer
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2 * 72000, recombinant His-tagged enzyme, SDS-PAGE, 2 * 72822, sequence calculation
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monomer
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1 * 72000, SDS-PAGE, 1 * 71705, sequence calculation
monomer
Pseudarthrobacter chlorophenolicus A6 / DSM 12829
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1 * 72000, SDS-PAGE, 1 * 71705, sequence calculation
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additional information
the active pocket in the enzyme is surrounded by A, B, and B' domains. The A domain serves as a catalytic domain and has the typical (beta/alpha)8-barrel structure of the GH13 family. The B' domain includes oligosaccharide binding sites, and both the B and B' domains of the enzyme contain acceptor subsites (+2, +3, +4, +5, and +6)
additional information
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the active pocket in the enzyme is surrounded by A, B, and B' domains. The A domain serves as a catalytic domain and has the typical (beta/alpha)8-barrel structure of the GH13 family. The B' domain includes oligosaccharide binding sites, and both the B and B' domains of the enzyme contain acceptor subsites (+2, +3, +4, +5, and +6)
additional information
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the putative enzyme interface is primarily mediated by two regions from domain N, residues Thr22, Leu25, Arg26, Arg29 and Tyr30 and residues Glu73, Leu76 and Leu77, which are involved in hydrophobic interactions with the corresponding residues from the second protomer
additional information
three-dimensional structure analysis. Structure comparison with the amylosucrase from Deinococcus geothermalis, overview
additional information
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three-dimensional structure analysis. Structure comparison with the amylosucrase from Deinococcus geothermalis, overview
additional information
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amylosucrases adopt a deep pocket topology of about 15 A with the catalytic triad located at the bottom
additional information
the active pocket in the enzyme is surrounded by A, B, and B' domains. The A domain serves as a catalytic domain andhas the typical (beta/alpha)8-barrel structure of the GH13 family. The B' domain includes oligosaccharide binding sites, and both the B and B' domains of the enzyme contain acceptor subsites (+2, +3, +4, +5, and +6)
additional information
-
the active pocket in the enzyme is surrounded by A, B, and B' domains. The A domain serves as a catalytic domain andhas the typical (beta/alpha)8-barrel structure of the GH13 family. The B' domain includes oligosaccharide binding sites, and both the B and B' domains of the enzyme contain acceptor subsites (+2, +3, +4, +5, and +6)
additional information
the residues forming subsites -1 and +1 are considered to be likely involved in the activity as well as the overall stability of the enzyme, active site structure, overview
additional information
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the residues forming subsites -1 and +1 are considered to be likely involved in the activity as well as the overall stability of the enzyme, active site structure, overview
additional information
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structure homology modeling based on the crystal structures of Neisseria poylsaccharea and Deinococcus geothermalis, structural differences and dynamics. The enzyme from Arthrobacter chlorophenolicus can be divided into two regions of different moving directions, predicted unfolding pathway, overview
