Aminometiltransferaza

Aminometiltransferaza
	Kristalna struktura ljudskog AMT.
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
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
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

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

\rightleftharpoons

[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 (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.

Literatura

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.

Vanjske veze

MeSH aminomethyltransferase

<!Metiltransferaze>

[pmid16051266-1] 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.

[2] 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.

[3] 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.

[4] 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.

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p r u Proteini: enzimi
Teme	Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
Tipovi	EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6