Aminometiltransferaza
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Aminometiltransferaza | |||||||||
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Identifikatori | |||||||||
EC broj | 2.1.2.10 | ||||||||
CAS broj | 37257-08-2 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
Ontologija gena | AmiGO / EGO | ||||||||
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Aminometiltransferaza | |
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Kristalna struktura ljudskog AMT.[1] | |
Identifikatori | |
Simbol | AMT |
Entrez | 275 |
Hugo | AMT 473 AMT |
OMIM | 238310 |
PDB | 1WSR |
RefSek | NM_000481 |
UniProt | P48728 |
Drugi podaci | |
EC broj | 2.1.2.10 |
Lokus | Hrom. 3 p21.2-21.1 |
Aminometiltransferaza (EC 2.1.2.10, S-aminometildihidrolipoilprotein:(6S)-tetrahidrofolat aminometiltransferaza (formira amonijak), T-protein, glicinska sintaza, tetrahidrofolatna aminometiltransferaza, (protein)-8-S-aminometildihidrolipoillizin:tetrahidrofolat aminometiltransferaza (formira amonijak)) je enzim sa sistematskim imenom (protein)-S8-aminometildihidrolipoillizin:tetrahidrofolat aminometiltransferaza (formira amonijak).[2][3][4] Aminometiltransferaza kataboliše formiranje metilentetrahidrofolata. Ona je deo kompleksa glicin dekarboksilaze.
- [protein]-S8-aminometildihidrolipoilizin tetrahidrofolat [protein]-dihidrolipoilizin 5,10-metilintetrahidrofolat NH3
- ↑ PDB 1WSR; Okamura-Ikeda K, Hosaka H, Yoshimura M, Yamashita E, Toma S, Nakagawa A, Fujiwara K, Motokawa Y, Taniguchi H (September 2005). „Crystal structure of human T-protein of glycine cleavage system at 2.0 A resolution and its implication for understanding non-ketotic hyperglycinemia”. Journal of Molecular Biology 351 (5): 1146–59. DOI:10.1016/j.jmb.2005.06.056. PMID 16051266.
- ↑ Okamura-Ikeda, J., Fujiwara, K. and Motokawa, Y. (1982). „Purification and characterization of chicken liver T protein, a component of the glycine cleavage system”. J. Biol. Chem. 257: 135-139. PMID 7053363.
- ↑ Perham, R.N. (2000). „Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions”. Annu. Rev. Biochem. 69: 961-1004. PMID 10966480.
- ↑ Nesbitt, N.M., Baleanu-Gogonea, C., Cicchillo, R.M., Goodson, K., Iwig, D.F., Broadwater, J.A., Haas, J.A., Fox, B.G. and Booker, S.J. (2005). „Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase”. Protein Expr. Purif. 39: 269-282. PMID 15642479.
- 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.
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