From Wikipedia, the free encyclopedia
3-deoxy-D-manno-octulosonic acid kinase
Identifiers
EC no. 2.7.1.166
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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.

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.
From Wikipedia, the free encyclopedia
3-deoxy-D-manno-octulosonic acid kinase
Identifiers
EC no. 2.7.1.166
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

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.

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.

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