AMP deaminaza

AMP deaminaza
	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
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

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

\rightleftharpoons

IMP + NH₃

Povezano

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

[1] 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.

[2] 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.

[3] Lee, Y.-P. (1957). „5′-Adenylic acid deaminase. II. Homogeneity and physicochemical properties”. J. Biol. Chem. 227: 993-998. PMID 13463020.

[4] Lee, Y.-P. (1957). „5′-Adenylic acid deaminase. III. Properties and kinetic studies”. J. Biol. Chem. 227: 999-1007. PMID 13463021.

[5] 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.

[6] Turner, D.H. and Turner, J.F. (1961). „Adenylic deaminase of pea seeds”. Biochem. J. 79: 143-147. PMID 13778717.

[7] Weil-Malherbe, W. and Green, R.H. (1955). „Ammonia formation in brain. 2. Brain adenylic deaminase”. Biochem. J. 61: 218-224. PMID 13260201.

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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