Aminometiltransferaza
| Aminometiltransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.1.2.10 | ||||||||
| CAS broj | 37257-08-2 | ||||||||
| 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 | ||||||||
| Ontologija gena | AmiGO / EGO | ||||||||
| |||||||||
| Aminometiltransferaza | |
|---|---|
 Kristalna struktura ljudskog AMT.[1] | |
| Identifikatori | |
| Simbol | AMT |
| Entrez | 275 |
| HUGO | AMT 473 AMT |
| OMIM | 238310 |
| PDB | 1WSR |
| RefSeq | NM_000481 |
| UniProt | P48728 |
| Ostali podaci | |
| EC broj | 2.1.2.10 |
| Lokus | Hromozom 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
Reference
- ^ PDB: 1WSR; Okamura-Ikeda K, Hosaka H, Yoshimura M, Yamashita E, Toma S, Nakagawa A, Fujiwara K, Motokawa Y, Taniguchi H (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. PMID 16051266. doi:10.1016/j.jmb.2005.06.056.
- ^ 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. CS1 одржавање: Вишеструка имена: списак аутора (веза)
- ^ 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. CS1 одржавање: Вишеструка имена: списак аутора (веза)
Literatura
- 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.
- William P. Jencks (1987). Catalysis in Chemistry and Enzymology. Dover Publications. ISBN 0486654605.
Spoljašnje veze
- aminomethyltransferase на US National Library of Medicine Medical Subject Headings (MeSH)
- п
- р
- у
Transferaze: jednougljenične transferaze (EC 2.1)
| N- | |
|---|---|
| O- | |
| Homocistein | |
| Drugi |
formil- i srodne grupe
| Hidroksimetiltransferaza | |
|---|---|
| Formiltransferaza | |
| Drugi |
|
i karbamoil
| Karboksi | |
|---|---|
| Karbamoil |
- Arginin:glicin amidinotransferaza
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