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Adenosine monophosphate deaminase 3

AMP Deaminase
catalyzes the conversion of AMP to IMP [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: ACID, CAN, HAD, V1a, FasT
Papers on AMP Deaminase
Safety evaluation of AMP deaminase from Aspergillus oryzae.
Roberts et al., Japan. In Food Chem Toxicol, Dec 2015
AMP deaminase showed no evidence of genotoxicity in the in vitro tests.
Structure-function relationships in mammalian histidine-proline-rich glycoprotein.
Raggi et al., Pisa, Italy. In Biochimie, Nov 2015
This observation provides a structural basis to the function of HPRG as an intracellular zinc chaperone which has been suggested by the involvement of the protein in the maintenance of the quaternary structure of skeletal muscle AMP deaminase (AMPD).
Sodium nitrite-induced oxidative stress causes membrane damage, protein oxidation, lipid peroxidation and alters major metabolic pathways in human erythrocytes.
Mahmood et al., Alīgarh, India. In Toxicol In Vitro, Oct 2015
However, there was a significant increase in acid phosphatase and also AMP deaminase, a marker of erythrocyte oxidative stress.
A continuous spectrophotometric assay for monitoring adenosine 5'-monophosphate production.
First, Shreveport, United States. In Anal Biochem, Sep 2015
Specifically, we have coupled the conversion of AMP to inosine 5'-monophosphate (IMP) (by AMP deaminase) to the oxidation of IMP (by IMP dehydrogenase).
Inhibition of AMP deaminase as therapeutic target in cardiovascular pathology.
Smolenski et al., Gdańsk, Poland. In Pharmacol Rep, Aug 2015
AMP deaminase (AMPD; EC catalyzes hydrolysis of the amino group from the adenine ring of AMP resulting in production of inosine 5'-monophosphate (IMP) and ammonia.
HIF-1α in the heart: remodeling nucleotide metabolism.
Wright et al., Johnson City, United States. In J Mol Cell Cardiol, May 2015
We find that AMP deaminase (AMPD), the entry point of the purine nucleotide cycle (PNC), is induced by HIF-1α at the level of mRNA, protein, and activity.
Altered AMP deaminase activity may extend postmortem glycolysis.
Gerrard et al., Blacksburg, United States. In Meat Sci, Apr 2015
We hypothesized that slowing adenonucleotide removal by reducing AMP deaminase activity would extend glycolysis and lower the ultimate pH of muscle.
Excessive degradation of adenine nucleotides by up-regulated AMP deaminase underlies afterload-induced diastolic dysfunction in the type 2 diabetic heart.
Miura et al., Sapporo, Japan. In J Mol Cell Cardiol, Mar 2015
The decline in ATP by pressure overloading in OLETF was associated with increased inosine 5-monophosphate and decreased adenosine levels, being consistent with the 2.5-times higher activity of cardiac AMP deaminase in OLETF.
AMPD1 regulates mTORC1-p70 S6 kinase axis in the control of insulin sensitivity in skeletal muscle.
Morisaki et al., Suita, Japan. In Bmc Endocr Disord, 2014
AMPD1, an isoform of AMP deaminase (AMPD), is suggested to play roles in the regulation of glucose metabolism through controlling AMP-activated protein kinase (AMPK) activation.
Opposing activity changes in AMP deaminase and AMP-activated protein kinase in the hibernating ground squirrel.
Johnson et al., Aurora, United States. In Plos One, 2014
We hypothesized that this switch might be determined by AMP and the dominance of opposing effects: metabolism through AMP deaminase (AMPD2) (summer) and activation of AMP-activated protein kinase (AMPK) (winter).
AMP deaminase 1 gene polymorphism and heart disease-a genetic association that highlights new treatment.
Barton et al., Gdańsk, Poland. In Cardiovasc Drugs Ther, 2014
Several studies identified that polymorphism of AMP deaminase 1 gene (AMPD1), in particular the common C34T variant of this gene was found to benefit patients with heart failure and ischemic heart disease.
AMPD1: a novel therapeutic target for reversing insulin resistance.
Morisaki et al., Suita, Japan. In Bmc Endocr Disord, 2013
A recent report that metformin, a drug known to reverse insulin resistance, demonstrated in vitro the metformin can inhibit AMP deaminase (AMPD) activity.
The role of histidine-proline-rich glycoprotein as zinc chaperone for skeletal muscle AMP deaminase.
Raggi et al., Pisa, Italy. In Biomolecules, 2013
We propose that the complex formed in skeletal muscle by the Zn2+ metalloenzyme AMP deaminase (AMPD) and the metal binding protein histidine-proline-rich glycoprotein (HPRG) acts in this manner.
Novel trends in the treatment of cardiovascular disorders: site- and event- selective adenosinergic drugs.
Nánási et al., Debrecen, Hungary. In Curr Med Chem, 2010
We discuss the chemical, pharmacological and clinical features of these compounds: (1) inhibitors of membrane adenosine transporters (NBTI, dipyridamole), (2) inhibitors of adenosine deaminase (coformycin, EHNA), (3) inhibitors of adenosine kinase (tubercidin, aristeromycin), (4) inhibitors of AMP deaminase (GP3269), (5) activators of 5'-nucleotidase (methotrexate), (6) adenosine regulators (acadesine) and (7) allosteric adenosine receptor modulators (PD81723, LUF6000).
Isolation and properties of AMP deaminase from jumbo squid (Dosidicus gigas) mantle muscle from the Gulf of California, Mexico.
Gollas-Galvan et al., Hermosillo, Mexico. In Food Chem, 2008
Isoelectric focusing of this enzyme showed a pI of 5.76, which agrees with pI values of AMP deaminase from other invertebrate organisms.
Membrane association, mechanism of action, and structure of Arabidopsis embryonic factor 1 (FAC1).
Phillips et al., Madison, United States. In J Biol Chem, 2006
analysis of the association between Arabidopsis FAC1 globular catalytic domain and intracellular membranes, with N-terminal transmembrane and disordered linker regions serving as the anchor and attachment to the globular catalytic domain
Crystallization and preliminary X-ray crystallographic analysis of adenosine 5'-monophosphate deaminase (AMPD) from Arabidopsis thaliana in complex with coformycin 5'-phosphate.
Phillips et al., Madison, United States. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2005
preliminary X-ray crystallographic structure of adenosine 5'-monophosphate deaminase
EMBRYONIC FACTOR 1 encodes an AMP deaminase and is essential for the zygote to embryo transition in Arabidopsis.
Liu et al., Wageningen, Netherlands. In Plant J, 2005
FAC1 is involved in early embryo development, most likely in providing sufficient ATP for embryo development to proceed beyond the zygote stage. [FAC1] [EMBRYONIC FACTOR 1]
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