Glicin amidinotransferaza
Glicin amidinotransferaza (EC 2.1.4.1, arginin-glicinska amidinotransferaza, arginin-glicinska transamidinaza, glicinska transamidinaza) je enzim sa sistematskim imenom L-arginin:glicin amidinotransferaza.[2][3][4][5][6][7][8][9] Ovaj enzim katalizuje sledeću hemijsku reakciju
| Glicin amidinotransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
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| Stereo pogled na AGAT u standardnoj orijentaciji[1] | |||||||||
| Identifikatori | |||||||||
| EC broj | 2.1.4.1 | ||||||||
| CAS broj | 9027-35-4 | ||||||||
| 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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- L-arginin + glicin L-ornitin + guanidinoacetat
Ovaj enzim može da koristi kanavanine umesto arginina.
Reference uredi
- ↑ Humm A, Fritsche E, Steinbacher S, Huber R (June 1997). „Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis”. EMBO J. 16 (12): 3373–85. DOI:10.1093/emboj/16.12.3373. PMC 1169963. PMID 9218780.
- ↑ Borsook, H. and Dubnoff, J.W. (1941). „The formation of glycocyamine in animal tissues”. J. Biol. Chem. 138: 389-403.
- ↑ Conconi, F. and Grazi, E. (1965). „Transamidinase of hog kidney. I. Purification and properties”. J. Biol. Chem. 240: 2461-2464. PMID 14304853.
- ↑ McGuire, D.M., Tormanen, C.D., Segal, I.S. and van Pilsum, J.F. (1980). „The effect of growth hormone and thyroxine on the amount of L-arginine:glycine amidinotransferase in kidneys of hypophysectomized rats, purification and some properties of rat kidney transamidinase”. J. Biol. Chem. 255: 1152-1159. PMID 6766137.
- ↑ Ratner, S. (1962). „Transamidination”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 6 (2nd izd.). New York: Academic Press. str. 267-275.
- ↑ Ratner, S. and Rochovansky, O. (1956). „Biosynthesis of guanidinoacetic acid. I. Purification and properties of transamidinase”. Arch. Biochem. Biophys. 63: 277-295. PMID 13355454.
- ↑ Ratner, S. and Rochovansky, O. (1956). „Biosynthesis of guanidinoacetic acid. II. Mechanism of amidine group transfer”. Arch. Biochem. Biophys. 63: 296-315. PMID 13355455.
- ↑ Walker, J.B. (1956). „Biosynthesis of arginine from canavanine and ornithine in kidney”. J. Biol. Chem. 218: 549-556. PMID 13278360.
- ↑ Walker, J.B. (1957). „Studies on the mechanism of action of kidney transamidinase”. J. Biol. Chem. 224: 57-66. PMID 13398387.
Literatura uredi
- 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.
- Ratner, S. (1962). „Transamidination”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 6 (2nd izd.). New York: Academic Press. str. 267-275.