6 lysine residues are critical for the pH-dependent positive homotropic cooperativity behaviour of the enzyme, the lysines form a regulatory anionic site to which AMP must bind to stimulate the enzyme at alkaline pH
connection between the operation of the hypothesized anionic activating site, responsible for positive homotropic cooperativity, and the inhibition exerted by anionic compounds that compete for the same site, among them ATP is most efficient, no inhibition of the trinitrobenzene sulfonic acid-desensitized enzyme
competitive inhibitor of the term placenta enzyme, AMP-deaminase from preterm placenta is not inhibited by physiological concentrations of orthophosphate at low substrate concentration range in contrast to the enzyme from the term organ
limited cleavage increases enzyme activity in presence of low concentrations of K+, probably due to removal of a fragment from the enzyme, which holds the enzyme in an inactive state, cleavage occurs e.g. during storage of both the muscle and the purified enzyme
at pH 7.0 the reaction catalysed by AMP-deaminase from human preterm placenta follows a well depicted sigmoid-shaped kinetic profile, with a half-saturation constant (S0.5) value of about 9.2 mM. Phosphate hardly influences the kinetic profile diminishing the S0.5 constant value slightly to 8.1 mM. Addition into the medium of 1 mM adenine nucleotide, ADP or ATP, transforms the sigmoid-shaped profile of the control kinetic curve into a hyperbolic one, diminishing simultaneously the value of the S0.5 constant from 9.2 mM to 2.4 mM, respectively. Kinetic analysis, overview
non significant differences in enzyme activity are observed between homogenates from HCC tumor fragments and tumor surrounding fragments of the liver, where the specific activity is about 0.077 micromole/min/mg of protein
significantly increased FAC1 expression in the zygote, early embryo and endosperm. During somatic embryogenesis, a high level of FAC1 expression is observed in developing embryos including putative embryogenic cells. FAC1 represents one of the earliest expressed genes known in plants. It may act through AMP depletion to provide sufficient energy for the zygote to proceed through development
AMP deaminase 3 is mutated in one of the mutant clones resistant to anthrax lethal toxin-induced death, AMPD3 deficiency does not affect anthrax lethal toxin entering cells and the cleavage of mitogen-activated protein kinase kinase by lethal factor inside cells, but does impair a downstream event that is linked to cell death. Restoration of anthrax lethal toxin sensitivity with ectopic reconstitution of AMPD3 expression
in contrast to AMP-deaminase isolated from the normal, healthy liver, where presence of relatively large (68 kDa) protein fragment is also detected, only smaller protein fragments are identified, while SDS-PAGE of AMP-deaminase isolated from the cirrhotic liver is performed
in enzyme from healthy liver beside immunologically reactive 92000 Da protein fragment, corresponding to the full size of the enzyme subunit, also a smaller, immunologically reactive protein fragment 68000 Da is identified in the gel. When SDS-PAGE of AMP-deaminase isolated from neo-plasmatic liver is performed only presence of protein fragment 68000 Da was detected
enzyme contains a histidine-proline-rich-glycoprotein HPRG component, bound via its catalytic subunit in a protein-protein complex, which is critical for the enzyme stability, disulfide bridges are involved in formation of enzyme conformation
heating in the presence of low KCl (150 mM) results in a rapid loss in activity with only 25% of initial activity being left after 30 min, about half of the initial activity remains after heating for 30 min in 25 mM histidine solution, solution, incubation in imidazole or phosphate solutions results in greater stability over 30 min of heating with AMPD activity decreasing by about 20%
both native enzyme and its histidine-proline-rich-glycoprotein HPRG component, the latter being completely separated from the enzyme and its catalytic subunit by Zn2+-affinity chromatography including presence of 1 M KCl
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AMP deaminase in the liver is elevated by 4.2fold in models of hepatotoxic injury as compared with controls. In acute hyperammonemia, activity of AMP deaminase increases by 59% in the neocortex. In the hippocampus of hyperammonemic rats, AMP deaminase activity is increased by 48%. Subacute hepatitis leads to 228% increase in AMP deaminase activity
during pregnancy the activity of AMP-deaminase in developing human placenta gradually decreases, being in homogenates of mature, term placenta (about 40 weeks of gestation) one fourth to one third of that in homogenates of immature (about 25 weeks of gestation) organ
the C34T T allele of the adenosine monophosphate deaminase-1 gene is associated with improved outcome in patients with cardiac dysfunction. Possession of the adenosine monophosphate deaminase-1 T allele is associated with decreased inotropic requirements before heart donation
Ranieri-Raggi, M.; Martini, D.; Sabbatini, A.R.; Moir, A.J.; Raggi, A.
Isolation by zinc-affinity chromatography of the histidine-proline-rich-glycoprotein molecule associated with rabbit skeletal muscle AMP deaminase. Evidence that the formation of a protein-protein complex between the catalytic subunit and the novel component is critical for the stability of the enzyme
Skladanowski, A.C.; Stepnowski, P.; Kleszczynski, K.; Dmochowska, B.
AMP deaminase in vitro inhibition by xenobiotics a potential molecular method for risk assessment of synthetic nitro- and polycyclic musks, imidazolium ionic liquids and N-glucopyranosyl ammonium salts