D-treoninska aldolaza
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| D-treoninska aldolaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 4.1.2.42 | ||||||||
| 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-treoninska aldolaza (EC 4.1.2.42, D-TA, DTA, nisko specifična D-TA, nisko specifična D-treoninska aldolaza) je enzim sa sistematskim imenom D-treonin acetaldehid-lijaza (formira glicin).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- (1) D-treonin glicin + acetaldehid
- (2) D-alotreonin glicin + acetaldehid
Ovaj piridoksal-fosfatni protein aktiviraju divalentni metalni katjoni (e.g. Co2+, Ni2+, Mn2+ or Mg2+).
Reference[uredi | uredi kod]
- ↑ Kataoka, M., Ikemi, M., Morikawa, T., Miyoshi, T., Nishi, K., Wada, M., Yamada, H. and Shimizu, S. (1997). „Isolation and characterization of D-threonine aldolase, a pyridoxal-5′-phosphate-dependent enzyme from Arthrobacter sp. DK-38”. Eur. J. Biochem. 248: 385-393. PMID 9346293.
- ↑ Liu, J.Q., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H. (1998). „A novel metal-activated pyridoxal enzyme with a unique primary structure, low specificity D-threonine aldolase from Arthrobacter sp. Strain DK-38. Molecular cloning and cofactor characterization”. J. Biol. Chem. 273: 16678-16685. PMID 9642221.
- ↑ Liu, J.Q., Odani, M., Dairi, T., Itoh, N., Shimizu, S. and Yamada, H. (1999). „A new route to L-threo-3-[4-(methylthio)phenylserine, a key intermediate for the synthesis of antibiotics: recombinant low-specificity D-threonine aldolase-catalyzed stereospecific resolution”]. Appl. Microbiol. Biotechnol. 51: 586-591. PMID 10390816.
- ↑ Liu, J.Q., Odani, M., Yasuoka, T., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H. (2000). „Gene cloning and overproduction of low-specificity D-threonine aldolase from Alcaligenes xylosoxidans and its application for production of a key intermediate for parkinsonism drug”. Appl. Microbiol. Biotechnol. 54: 44-51. PMID 10952004.
- ↑ Liu, J.Q., Dairi, T., Itoh, N., Kataoka, M., Shimizu, S. and Yamada, H. (2000). „Diversity of microbial threonine aldolases and their application”. J. Mol. Catal. B 10: 107-115.
- ↑ Paiardini, A., Contestabile, R., D'Aguanno, S., Pascarella, S. and Bossa, F. (2003). „Threonine aldolase and alanine racemase: novel examples of convergent evolution in the superfamily of vitamin B6-dependent enzymes”. Biochim. Biophys. Acta 1647: 214-219. PMID 12686135.
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.