2.3.1.210: dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase
This is an abbreviated version!
For detailed information about dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase, go to the full flat file.
Word Map on EC 2.3.1.210
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2.3.1.210
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ubiquitin-conjugating
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htert
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telomerase
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esophageal
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radiosensitivity
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radioresistance
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proteasome
- 2.3.1.210
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ubiquitin-conjugating
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htert
- telomerase
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esophageal
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radiosensitivity
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radioresistance
- proteasome
Reaction
Synonyms
RffC, TDP-fucosamine acetyltransferase, WecD
ECTree
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General Information
General Information on EC 2.3.1.210 - dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase
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evolution
physiological function
additional information
WecD is a GNAT family member. The GNAT N-acetyltransferase fold is common to a number of enzymes involved in acetylation of histones, aminoglycoside antibiotics, serotonin, and sugars
evolution
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WecD is a GNAT family member. The GNAT N-acetyltransferase fold is common to a number of enzymes involved in acetylation of histones, aminoglycoside antibiotics, serotonin, and sugars
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the enzyme is involved in biosynthesis of enterobacterial common antigen, ECA, a polysaccharide found on the outer membrane of virtually all Gram-negative enteric bacteria, that consists of three sugars, N-acetyl-D-glucosamine, N-acetyl-D-mannosaminuronic acid, and 4-acetamido-4,6-dideoxy-D-galactose, organized into trisaccharide repeating units having the sequence ->3)-alpha-D-Fuc4NAc-(1->4)-beta-D-ManNAcA-(1->4)-alpha-D-GlcNAc-(1->
physiological function
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the enzyme is involved in biosynthesis of enterobacterial common antigen, ECA, a polysaccharide found on the outer membrane of virtually all Gram-negative enteric bacteria, that consists of three sugars, N-acetyl-D-glucosamine, N-acetyl-D-mannosaminuronic acid, and 4-acetamido-4,6-dideoxy-D-galactose, organized into trisaccharide repeating units having the sequence ->3)-alpha-D-Fuc4NAc-(1->4)-beta-D-ManNAcA-(1->4)-alpha-D-GlcNAc-(1->
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usage of flexible docking to generate a WecD-bound model of the acetyl-CoATDP-fucosamine tetrahedral intermediate, representing the structure during acetyl transfer. that WecD does not possess a residue that directly functions as a catalytic base, although Tyr208 is well positioned to function as a general acid by protonating the thiolate anion of CoA, modeling of TDP-D-Fuc4N:acetyl-CoA transition state bound to WecD, overview. The WecD tetrahedral intermediate results from nucleophilic attack of the 4-amino group of TDP-fucosamine at the acetyl-CoA thioester carbon atom
additional information
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usage of flexible docking to generate a WecD-bound model of the acetyl-CoATDP-fucosamine tetrahedral intermediate, representing the structure during acetyl transfer. that WecD does not possess a residue that directly functions as a catalytic base, although Tyr208 is well positioned to function as a general acid by protonating the thiolate anion of CoA, modeling of TDP-D-Fuc4N:acetyl-CoA transition state bound to WecD, overview. The WecD tetrahedral intermediate results from nucleophilic attack of the 4-amino group of TDP-fucosamine at the acetyl-CoA thioester carbon atom
additional information
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usage of flexible docking to generate a WecD-bound model of the acetyl-CoATDP-fucosamine tetrahedral intermediate, representing the structure during acetyl transfer. that WecD does not possess a residue that directly functions as a catalytic base, although Tyr208 is well positioned to function as a general acid by protonating the thiolate anion of CoA, modeling of TDP-D-Fuc4N:acetyl-CoA transition state bound to WecD, overview. The WecD tetrahedral intermediate results from nucleophilic attack of the 4-amino group of TDP-fucosamine at the acetyl-CoA thioester carbon atom
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