AMP deaminaza
AMP deaminaza | |||||||||
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AMP deaminaza dimer, Arabidopsis thaliana | |||||||||
Identifikatori | |||||||||
EC broj | 3.5.4.6 | ||||||||
CAS broj | 2602636 | ||||||||
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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AMP deaminaza (EC 3.5.4.6, adenilno kiselinska deaminaza, AMP aminaza, adenilna deaminaza, adenilatna deaminaza, 5-AMP deaminaza, adenozin 5-monofosfatna deaminaza, 5-adenilatna deaminaza, adenilna deaminaza, 5-adenilno kiselinska deaminaza, adenozinska monofosfatna deaminaza, adenilatna aminohidrolaza, adenilatna desaminaza, adenozin 5-fosfatna aminohidrolaza, 5-adenilatna deaminaza) je enzim sa sistematskim imenom AMP aminohidrolaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- AMP + H2O IMP + NH3
Vidi još
- EC 3.5.4.17, adenozin-fosfat deaminaza.
Reference
- ↑ Kalckar, H.M. (1947). „Differential spectrophotometry of purine compounds by means of specific enzymes. III. Studies of the enzymes of purine metabolism”. J. Biol. Chem. 167: 461-475.
- ↑ Lee, Y.-P. (1957). „5′-Adenylic acid deaminase. I. Isolation of the crystalline enzyme from rabbit skeletal muscle”. J. Biol. Chem. 227: 987-992. PMID 13463019.
- ↑ Lee, Y.-P. (1957). „5′-Adenylic acid deaminase. II. Homogeneity and physicochemical properties”. J. Biol. Chem. 227: 993-998. PMID 13463020.
- ↑ Lee, Y.-P. (1957). „5′-Adenylic acid deaminase. III. Properties and kinetic studies”. J. Biol. Chem. 227: 999-1007. PMID 13463021.
- ↑ Mendicino, J. and Muntz, J.A. (1958). „The activating effect of adenosine triphosphate on brain adenylic deaminase”. J. Biol. Chem. 233: 178-183. PMID 13563464.
- ↑ Turner, D.H. and Turner, J.F. (1961). „Adenylic deaminase of pea seeds”. Biochem. J. 79: 143-147. PMID 13778717.
- ↑ Weil-Malherbe, W. and Green, R.H. (1955). „Ammonia formation in brain. 2. Brain adenylic deaminase”. Biochem. J. 61: 218-224. PMID 13260201.
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 AMP+deaminase
- p
- r
- u
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
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