(KDO)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase

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(KDO)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase
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EC no. 2.4.99.15
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(KDO)3-lipid IVA (2-4) 3-deoxy-D-manno-octulosonic acid transferase (EC 2.4.99.15, KDO transferase, waaA (gene), kdtA (gene), 3-deoxy-D-manno-oct-2-ulosonic acid transferase, 3-deoxy-manno-octulosonic acid transferase) is an enzyme with systematic name CMP-3-deoxy-D-manno-oct-2-ulosonate:(KDO)3-lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase ((2->4) glycosidic bond-forming). [1] [2] This enzyme catalyses the following chemical reaction

alpha-Kdo-(2->8)-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP-alpha-Kdo alpha-Kdo-(2->8)-[alpha-Kdo-(2->4)]-alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-lipid IVA + CMP

The enzyme from Chlamydia psittaci transfers four KDO residues to lipid A, forming a branched tetrasaccharide.

Related Research Articles

WAAA may refer to:

In enzymology, a 3-deoxy-manno-octulosonate cytidylyltransferase is an enzyme that catalyzes the chemical reaction

3-Deoxy-<small>D</small>-<i>manno</i>-oct-2-ulosonic acid Chemical compound

3-Deoxy-d-manno-oct-2-ulosonic acid is an ulosonic acid of a 2-ketooctose which is used by bacteria in the synthesis of lipopolysaccharides. The d-manno prefix indicates that the four chiral centers have the same configuration as d-mannose.

<span class="mw-page-title-main">Saccharolipid</span> Class of chemical compounds

Saccharolipids are chemical compounds containing fatty acids linked directly to a sugar backbone, forming structures that are compatible with membrane bilayers. In the saccharolipids, a monosaccharide substitutes for the glycerol backbone present in glycerolipids and glycerophospholipids. The most familiar saccharolipids are the acylated glucosamine precursors of the lipid A component of the lipopolysaccharides in Gram-negative bacteria. Typical lipid A molecules are disaccharides of glucosamine, which are derivatized with as many as seven fatty-acyl chains. The minimal lipopolysaccharide required for growth in Escherichia coli is Kdo2-Lipid A, a hexa-acylated disaccharide of glucosamine (LipidA) that is glycosylated with two 3-deoxy-D-manno-octulosonic acid (Kdo) residues.

Core oligosaccharide is a short chain of sugar residues within Gram-negative lipopolysaccharide (LPS). Core-OS are highly diverse among bacterial species and even within strains of species

In molecular biology, the lipopolysaccharide kinase (Kdo/WaaP) family is a family of lipopolysaccharide kinases that includes lipopolysaccharide core heptose(I) kinase rfaP. Lipopolysaccharide core heptose(I) kinase rfaP is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that it is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of Salmonella enterica. The family also includes 3-deoxy-D-manno-octulosonic acid kinase from Haemophilus influenzae, which phosphorylates Kdo-lipid IV(A), a lipopolysaccharide precursor, and is involved in virulence.

<span class="mw-page-title-main">DAHP synthase</span> Class of enzymes

3-Deoxy-D-arabinoheptulosonate 7-phosphate (DAHP) synthase is the first enzyme in a series of metabolic reactions known as the shikimate pathway, which is responsible for the biosynthesis of the amino acids phenylalanine, tyrosine, and tryptophan. Since it is the first enzyme in the shikimate pathway, it controls the amount of carbon entering the pathway. Enzyme inhibition is the primary method of regulating the amount of carbon entering the pathway. Forms of this enzyme differ between organisms, but can be considered DAHP synthase based upon the reaction that is catalyzed by this enzyme.

2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase is an enzyme with systematic name L-aspartate 4-semialdehyde:1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate methylglyoxaltransferase. This enzyme catalyses the following chemical reaction

Lipid IVA 4-amino-4-deoxy-L-arabinosyltransferase is an enzyme with systematic name 4-amino-4-deoxy-alpha-L-arabinopyranosyl ditrans, octacis-undecaprenyl phosphate:lipid IVA 4-amino-4-deoxy-L-arabinopyranosyltransferase. This enzyme catalyses the following chemical reaction

Lipid IVA 3-deoxy-D-manno-octulosonic acid transferase is an enzyme with systematic name CMP-3-deoxy-D-manno-oct-2-ulosonate:lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase. This enzyme catalyses the following chemical reaction

KDO transferase may refer to:

WaaA (gene) may refer to:

KdtA may refer to:

3-deoxy-D-manno-oct-2-ulosonic acid transferase may refer to:

3-deoxy-manno-octulosonic acid transferase may refer to:

(KDO)-lipid IVA 3-deoxy-D-manno-octulosonic acid transferase is an enzyme with systematic name CMP-3-deoxy-D-manno-oct-2-ulosonate:(KDO)-lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase. This enzyme catalyses the following chemical reaction

(KDO)2-lipid IVA (2-8) 3-deoxy-D-manno-octulosonic acid transferase is an enzyme with systematic name CMP-3-deoxy-D-manno-oct-2-ulosonate:(KDO)2-lipid IVA 3-deoxy-D-manno-oct-2-ulosonate transferase . This enzyme catalyses the following chemical reaction

3-deoxy-D-manno-octulosonic acid kinase is an enzyme with systematic name ATP:(KDO)-lipid IVA 3-deoxy-alpha-D-manno-oct-2-ulopyranose 4-phosphotransferase. This enzyme catalyses the following chemical reaction

Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase is an enzyme with systematic name UDP-4-amino-4-deoxy-alpha-L-arabinose:ditrans,octacis-undecaprenyl phosphate 4-amino-4-deoxy-alpha-L-arabinosyltransferase. This enzyme catalyses the following chemical reaction

3-Deoxy-2-octulosonidase is an enzyme with systematic name capsular-polysaccharide 3-deoxy-D-manno-2-octulosonohydrolase. This enzyme catalyses the following chemical reaction

References

  1. Brabetz W, Lindner B, Brade H (September 2000). "Comparative analyses of secondary gene products of 3-deoxy-D-manno-oct-2-ulosonic acid transferases from Chlamydiaceae in Escherichia coli K-12". European Journal of Biochemistry. 267 (17): 5458–65. doi: 10.1046/j.1432-1327.2000.01619.x . PMID   10951204.
  2. Holst O, Bock K, Brade L, Brade H (April 1995). "The structures of oligosaccharide bisphosphates isolated from the lipopolysaccharide of a recombinant Escherichia coli strain expressing the gene gseA [3-deoxy-D-manno-octulopyranosonic acid (Kdo) transferase] of Chlamydia psittaci 6BC". European Journal of Biochemistry. 229 (1): 194–200. doi:10.1111/j.1432-1033.1995.tb20455.x. PMID   7744029.