Malonatna dekarboksilaza nezavisna od biotina
(Preusmjereno sa stranice Biotin-nezavisna malonatna dekarboksilaza)
| Biotin-nezavisna malonatna dekarboksilaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 4.1.1.88 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
| |||||||||
Biotin-nezavisna malonatna dekarboksilaza (EC 4.1.1.88, malonat dekarboksilaza (saout biotin), malonat dekarboksilaza, MDC) je enzim sa sistematskim imenom malonat karboksilijaza (biotin-nezavisna).[1][2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
- malonat + H+ acetat + CO2
Pozanat su dva tipa malonatne dekarboksilaze. Oba su multienzimski kompleksi.
Reference[uredi | uredi kod]
- ↑ Schmid, M., Berg, M., Hilbi, H. and Dimroth, P. (1996). „Malonate decarboxylase of Klebsiella pneumoniae catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A-like prosthetic group”. Eur. J. Biochem. 237: 221-228. PMID 8620876.
- ↑ Byun, H.S. and Kim, Y.S. (1997). „Subunit organization of bacterial malonate decarboxylases: the smallest δ subunit as an acyl-carrier protein”. J. Biochem. Mol. Biol. 30: 132-137.
- ↑ Hoenke, S., Schmid, M. and Dimroth, P. (1997). „Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli”. Eur. J. Biochem. 246: 530-538. PMID 9208947.
- ↑ Chohnan, S., Fujio, T., Takaki, T., Yonekura, M., Nishihara, H. and Takamura, Y. (1998). „Malonate decarboxylase of Pseudomonas putida is composed of five subunits”. FEMS Microbiol. Lett. 169: 37-43. PMID 9851033.
- ↑ Hoenke, S., Schmid, M. and Dimroth, P. (2000). „Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ancient class of nucleotidyltransferases”. Biochemistry 39: 13233-13240. PMID 11052676.
- ↑ Handa, S., Koo, J.H., Kim, Y.S. and Floss, H.G. (1999). „Stereochemical course of biotin-independent malonate decarboxylase catalysis”. Arch. Biochem. Biophys. 370: 93-96. PMID 10496981.
- ↑ Koo, J.H. and Kim, Y.S. (1999). „Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus”. Eur. J. Biochem. 266: 683-690. PMID 10561613.
- ↑ Kim, Y.S. (2002). „Malonate metabolism: biochemistry, molecular biology, physiology, and industrial application”. J. Biochem. Mol. Biol. 35: 443-451. PMID 12359084.
- ↑ Dimroth, P. and Hilbi, H. (1997). „Enzymic and genetic basis for bacterial growth on malonate”. Mol. Microbiol. 25: 3-10. PMID 11902724.
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.