D-aminokiselina transaminaza
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| D-aminokiselina transaminaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.6.1.21 | ||||||||
| CAS broj | 37277-85-3 | ||||||||
| 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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D-aminokiselina transaminaza (EC 2.6.1.21, D-aspartatna transaminaza, D-alaninska aminotransferaza, D-aspartinska aminotransferaza, D-alanin-D-glutamatna transaminaza, D-alaninska transaminaza, D-aminokiselinska aminotransferaza) je enzim sa sistematskim imenom D-alanin:2-oksoglutarat aminotransferaza.[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
- D-alanin + 2-oksoglutarat piruvat + D-glutamat
Ovaj enzim je piridoksal-fosfatni protein. Enzim iz termofilnih Bacillus vrsta deluje na mnoge D-aminokiseline. D-alanin i D-2-aminobutirat su najbolji amino donori.
Reference[uredi | uredi kod]
- ↑ Thorne, C.B., Gómez, C.G. and Housewright, R.D. (1955). „Transamination of D-amino acids by Bacillus subtilis”. J. Bacteriol. 69: 357-362. PMID 14367287.
- ↑ Thorne, C.B. and Molnar, D.M. (1955). „D-Amino acid transamination in Bacillus anthracis”. J. Bacteriol. 70: 420-426. PMID 13263311.
- ↑ Martinez-Carrion, M. and Jenkins, W.T. (1965). „D-Alanine-D-glutamate transaminase. I. Purification and characterization”. J. Biol. Chem. 240: 3538-3546. PMID 4953710.
- ↑ Ozawa, T., Fukuda, M. and Sasaoka, K. (1973). „Occurrence of D-amino acid aminotransferase in pea seedlings”. Biochem. Biophys. Res. Commun. 52: 998-1002. PMID 4710577.
- ↑ Yonaha, K., Misono, H., Yamamoto, T. and Soda, K. (1975). „D-Amino acid aminotransferase of Bacillus sphaericus. Enzymologic and spectrometric properties”. J. Biol. Chem. 250: 6983-6989. PMID 1158891.
- ↑ Tanizawa, K., Masu, Y., Asano, S., Tanaka, H. and Soda, K. (1989). „Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species. Purification, characterization, and active site sequence determination”. J. Biol. Chem. 264: 2445-2449. PMID 2914916.
- ↑ Fotheringham, I.G., Bledig, S.A. and Taylor, P.P. (1998). „Characterization of the genes encoding D-amino acid transaminase and glutamate racemase, two D-glutamate biosynthetic enzymes of Bacillus sphaericus ATCC 10208”. J. Bacteriol. 180: 4319-4323. PMID 9696787.
- ↑ van Ophem, P.W., Erickson, S.D., Martinez del Pozo, A., Haller, I., Chait, B.T., Yoshimura, T., Soda, K., Ringe, D., Petsko, G. and Manning, J.M. (1998). „Substrate inhibition of D-amino acid transaminase and protection by salts and by reduced nicotinamide adenine dinucleotide: isolation and initial characterization of a pyridoxo intermediate related to inactivation”. Biochemistry 37: 2879-2888. PMID 9485439.
- ↑ Sugio, S., Petsko, G.A., Manning, J.M., Soda, K. and Ringe, D. (1995). „Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity”. Biochemistry 34: 9661-9669. PMID 7626635.
Literatura[uredi | uredi kod]
- 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.