DTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase

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DTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase
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EC no. 2.3.1.209
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DTDP-4-amino-4,6-dideoxy-D-glucose acyltransferase (EC 2.3.1.209, VIOB) is an enzyme with systematic name acetyl-CoA:dTDP-4-amino-4,6-dideoxy-alpha-D-glucose N-acetyltransferase. [1] This enzyme catalyses the following chemical reaction

acetyl-CoA + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose CoA + dTDP-4-acetamido-4,6-dideoxy-alpha-D-glucose

4-acetamido-4,6-dideoxy-alpha-D-glucose is part of the O antigens of Shigella dysenteriae type 7 and Escherichia coli O7.

Related Research Articles

The enzyme dTDP-glucose 4,6-dehydratase (EC 4.2.1.46) catalyzes the chemical reaction

In enzymology, formate C-acetyltransferase is an enzyme. Pyruvate formate lyase is found in Escherichia coli and other organisms. It helps regulate anaerobic glucose metabolism. Using radical non-redox chemistry, it catalyzes the reversible conversion of pyruvate and coenzyme-A into formate and acetyl-CoA. The reaction occurs as follows:

In enzymology, a maltose O-acetyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Serine O-acetyltransferase</span>

In enzymology, a serine O-acetyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a dTDP-4-amino-4,6-dideoxy-D-glucose transaminase is an enzyme that catalyzes the chemical reaction

In enzymology, a dTDP-4-amino-4,6-dideoxygalactose transaminase is an enzyme that catalyzes the chemical reaction

DTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose N,N-dimethyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose 3-N,N-dimethyltransferase. This enzyme catalyses the following chemical reaction

DTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose N,N-dimethyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose 3-N,N-dimethyltransferase. This enzyme catalyses the following chemical reaction

DTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose 3-N-acetyltransferase is an enzyme with systematic name acetyl-CoA:dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose 3-N-acetyltransferase. This enzyme catalyses the following chemical reaction

UDP-2-acetamido-3-amino-2,3-dideoxy-glucuronate N-acetyltransferase is an enzyme with systematic name acetyl-CoA:UDP-2-acetamido-3-amino-2,3-dideoxy-alpha-D-glucuronate N-acetyltransferase. This enzyme catalyses the following chemical reaction

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase is an enzyme with systematic name acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine N-acetyltransferase. This enzyme catalyses the following chemical reaction

UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase is an enzyme with systematic name acetyl-CoA:UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine N-acetyltransferase. This enzyme catalyses the following chemical reaction

DTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase is an enzyme with systematic name acetyl-CoA:dTDP-4-amino-4,6-dideoxy-alpha-D-galactose N-acetyltransferase. This enzyme catalyses the following chemical reaction

DTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose transaminase is an enzyme with systematic name dTDP-3-amino-3,6-dideoxy-alpha-D-glucopyranose:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction

DTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose transaminase is an enzyme with systematic name dTDP-3-amino-3,6-dideoxy-alpha-D-galactopyranose:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction

UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine transaminase is an enzyme with systematic name UDP-4-amino-4,6-dideoxy-N-acetyl-alpha-D-glucosamine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction

UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine transaminase is an enzyme with systematic name UDP-4-amino-4,6-dideoxy-N-acetyl-beta-L-altrosamine:2-oxoglutarate aminotransferase. This enzyme catalyses the following chemical reaction

UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting) (EC 4.2.1.115, FlaA1, UDP-N-acetylglucosamine 5-inverting 4,6-dehydratase, PseB, UDP-N-acetylglucosamine hydro-lyase (inverting, UDP-2-acetamido-2,6-dideoxy-β-L)arabino-hex-4-ulose-forming)) is an enzyme with systematic name UDP-N-acetyl-α-D-glucosamine hydro-lyase (inverting; UDP-2-acetamido-2,6-dideoxy-β-L-arabino-hex-4-ulose-forming). This enzyme catalyses the following chemical reaction

TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase (dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose-forming) is an enzyme with systematic name dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose:dTDP-3-dehydro-6-deoxy-alpha-D-galactopyranose isomerase. This enzyme catalyses the following chemical reaction

The enterobacterial common antigen (ECA) is a carbohydrate antigen found in the outer membrane of many Enterobacterales species. The antigen is unanimously absent from other gram-negative and gram-positive bacteria. Aeromonas hydrophila 209A is the only organism outside of Enterobacterales that expresses the ECA. More studies are needed to explain the presence of the antigen in this species as no other strains of this species express the antigen. The ECA is a polysaccharide made of repeating units of trisaccharides. The functions of these units have very few proven functions. Some evidence indicates role in pathogenicity in the bacteria that present the ECA. There are three separate types of ECA these include ECAPG, ECALPS, and ECACYC, each have different lengths. The synthesis of the ECA is controlled by the wec operon and has a 12-step synthesis which is described below. Due to the lack of proven function of the ECA, any clinical significance is hard to define however, some evidence suggests that human serum has antibodies against ECA.

References

  1. ↑ Wang Y, Xu Y, Perepelov AV, Qi Y, Knirel YA, Wang L, Feng L (December 2007). "Biochemical characterization of dTDP-D-Qui4N and dTDP-D-Qui4NAc biosynthetic pathways in Shigella dysenteriae type 7 and Escherichia coli O7". Journal of Bacteriology. 189 (23): 8626–35. doi:10.1128/jb.00777-07. PMC   2168959 . PMID   17905981.
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