3-deoxy-D-manno-octulosonic acid kinase

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3-deoxy-D-manno-octulosonic acid kinase
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EC no. 2.7.1.166
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3-deoxy-D-manno-octulosonic acid kinase (EC 2.7.1.166, kdkA (gene), Kdo kinase) is an enzyme with systematic name ATP:(KDO)-lipid IVA 3-deoxy-alpha-D-manno-oct-2-ulopyranose 4-phosphotransferase. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

alpha-Kdo-(2->6)-lipid IVA + ATP 4-O-phospho-alpha-Kdo-(2->6)-lipid IVA + ADP

The enzyme phosphorylates the 4-OH position of KDO in (KDO)-lipid IVA.

Related Research Articles

WAAA may refer to:

In enzymology, a 3-deoxyoctulosonase (EC 3.2.1.144) is an enzyme that catalyzes the chemical reaction

<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.

<span class="mw-page-title-main">Haloacid dehydrogenase superfamily</span>

The haloacid dehydrogenase superfamily is a superfamily of enzymes that include phosphatases, phosphonatases, P-type ATPases, beta-phosphoglucomutases, phosphomannomutases, and dehalogenases, and are involved in a variety of cellular processes ranging from amino acid biosynthesis to detoxification.

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.

UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating) (EC 1.1.1.305, UDP-GlcUA decarboxylase, ArnADH) is an enzyme with systematic name UDP-glucuronate:NAD+ oxidoreductase (decarboxylating). This enzyme catalyses the following chemical reaction

UDP-4-amino-4-deoxy-L-arabinose formyltransferase is an enzyme with systematic name 10-formyltetrahydrofolate:UDP-4-amino-4-deoxy-beta-L-arabinose N-formyltransferase. 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

(KDO)3-lipid IVA (2-4) 3-deoxy-D-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 . 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

UDP-2,3-diacylglucosamine diphosphatase (EC 3.6.1.54, UDP-2,3-diacylglucosamine hydrolase, UDP-2,3-diacylglucosamine pyrophosphatase, ybbF (gene), lpxH (gene)) is an enzyme with systematic name UDP-2,3-bis((3R)-3-hydroxymyristoyl)-alpha-D-glucosamine 2,3-bis((3R)-3-hydroxymyristoyl)-beta-D-glucosaminyl 1-phosphate phosphohydrolase. This enzyme catalyses the following chemical reaction

N-glycosyltransferase is an enzyme in prokaryotes which transfers individual hexoses onto asparagine sidechains in substrate proteins, using a nucleotide-bound intermediary, within the cytoplasm. They are distinct from regular N-glycosylating enzymes, which are oligosaccharyltransferases that transfer pre-assembled oligosaccharides. Both enzyme families however target a shared amino acid sequence asparagine—-any amino acid except proline—serine or threonine (N–x–S/T), with some variations.

References

  1. Brabetz W, Müller-Loennies S, Brade H (November 2000). "3-Deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferase (WaaA) and kdo kinase (KdkA) of Haemophilus influenzae are both required to complement a waaA knockout mutation of Escherichia coli". The Journal of Biological Chemistry. 275 (45): 34954–62. doi: 10.1074/jbc.M005204200 . PMID   10952982.
  2. Harper M, Boyce JD, Cox AD, St Michael F, Wilkie IW, Blackall PJ, Adler B (August 2007). "Pasteurella multocida expresses two lipopolysaccharide glycoforms simultaneously, but only a single form is required for virulence: identification of two acceptor-specific heptosyl I transferases". Infection and Immunity. 75 (8): 3885–93. doi:10.1128/IAI.00212-07. PMC   1952014 . PMID   17517879.
  3. White KA, Kaltashov IA, Cotter RJ, Raetz CR (June 1997). "A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase and a Kdo kinase in extracts of Haemophilus influenzae". The Journal of Biological Chemistry. 272 (26): 16555–63. doi: 10.1074/jbc.272.26.16555 . PMID   9195966.
  4. White KA, Lin S, Cotter RJ, Raetz CR (October 1999). "A Haemophilus influenzae gene that encodes a membrane bound 3-deoxy-D-manno-octulosonic acid (Kdo) kinase. Possible involvement of kdo phosphorylation in bacterial virulence". The Journal of Biological Chemistry. 274 (44): 31391–400. doi: 10.1074/jbc.274.44.31391 . PMID   10531340.