3-dezoksi-D-mano-oktulozonska kiselina kinaza
3-dezoksi-D-mano-oktulozonska kiselina kinaza (EC 2.7.1.166, kdkA (gen), Kdo kinaza) je enzim sa sistematskim imenom ATP:(KDO)-lipid IVA 3-dezoksi-alfa-D-mano-okt-2-ulopiranoza 4-fosfotransferaza.[1][2][3][4] Ovaj enzim katalizuje sledeću hemijsku reakciju
3-dezoksi-D-mano-oktulozonska kiselina kinaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.7.1.166 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Ovaj enzim fosforiliše 4-OH poziciju KDO jedinice u (KDO)-lipidu IVA.
Reference uredi
- ↑ Brabetz, W., Muller-Loennies, S. and Brade, H. (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”. J. Biol. Chem. 275: 34954-34962. PMID 10952982.
- ↑ Harper, M., Boyce, J.D., Cox, A.D., St Michael, F., Wilkie, I.W., Blackall, P.J. and Adler, B. (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”. Infect. Immun. 75: 3885-3893. PMID 17517879.
- ↑ White, K.A., Kaltashov, I.A., Cotter, R.J. and Raetz, C.R. (1997). „A mono-functional 3-deoxy-D-manno-octulosonic acid (Kdo) transferase and a Kdo kinase in extracts of Haemophilus influenzae”. J. Biol. Chem. 272: 16555-16563. PMID 9195966.
- ↑ White, K.A., Lin, S., Cotter, R.J. and Raetz, C.R. (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”. J. Biol. Chem. 274: 31391-31400. PMID 10531340.
Literatura uredi
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.