Glicerat 2-kinaza
Glicerat 2-kinaza (EC 2.7.1.165, D-glicerat-2-kinaza, gliceratna kinaza (formira 2-fosfoglicerat), ATP:(R)-gliceratna 2-fosfotransferaza) je enzim sa sistematskim imenom ATP:D-glicerat 2-fosfotransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Glicerat 2-kinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.7.1.165 | ||||||||
| 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 ima ključnu ulogu u nefosforilativnom Entner-Doudorof putu kod arhaja.
Reference uredi
- ↑ Liu, B., Wu, L., Liu, T., Hong, Y., Shen, Y. and Ni, J. (2009). „A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties”. Biotechnol. Lett. 31: 1937-1941. PMID 19690808.
- ↑ Reher, M., Bott, M. and Schonheit, P. (2006). „Characterization of glycerate kinase (2-phosphoglycerate forming), a key enzyme of the nonphosphorylative Entner-Doudoroff pathway, from the thermoacidophilic euryarchaeon Picrophilus torridus”. FEMS Microbiol. Lett. 259: 113-119. PMID 16684110.
- ↑ Liu, B., Hong, Y., Wu, L., Li, Z., Ni, J., Sheng, D. and Shen, Y. (2007). „A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization”. Extremophiles 11: 733-739. PMID 17563835.
- ↑ Noh, M., Jung, J.H. and Lee, S.B. (2006). „Purification and characterization of glycerate kinase from the thermoacidophilic archaeon Thermoplasma acidophilum: an enzyme belonging to the second glycerate kinase family”. Biotechnol. Bioprocess Eng. 11: 344-350.
- ↑ Yoshida, T., Fukuta, K., Mitsunaga, T., Yamada, H. and Izumi, Y. (1992). „Purification and characterization of glycerate kinase from a serine-producing methylotroph, Hyphomicrobium methylovorum GM2”. Eur. J. Biochem. 210: 849-854. PMID 1336459.
- ↑ Hubbard, B.K., Koch, M., Palmer, D.R., Babbitt, P.C. and Gerlt, J.A. (1998). „Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli”. Biochemistry 37: 14369-14375. PMID 9772162.
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.