Glicerat 2-kinaza
| Glicerat 2-kinaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.7.1.165 | ||||||||
| Baze podataka | |||||||||
| IntEnz | IntEnz pregled | ||||||||
| BRENDA | BRENDA pristup | ||||||||
| ExPASy | NiceZyme pregled | ||||||||
| KEGG | KEGG pristup | ||||||||
| MetaCyc | metabolički put | ||||||||
| PRIAM | profil | ||||||||
| Strukture PBP | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
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
Ovaj enzim ima ključnu ulogu u nefosforilativnom Entner-Doudorof putu kod arhaja.
Reference
[уреди | уреди извор]- ^ 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
[уреди | уреди извор]- Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.
Spoljašnje veze
[уреди | уреди извор]- Glycerate+2-kinase на US National Library of Medicine Medical Subject Headings (MeSH)
