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1 ure of an N-truncated rabbit skeletal muscle AMP deaminase.
2 t is highly conserved in other adenosine and AMP deaminases.
3 een suggested that an acquired deficiency of AMP deaminase 1 (AMPD1) may be responsible for muscle we
4 ctivation of anaplerotic reactions driven by AMP deaminase 3 (Ampd3) and catabolism of branched-chain
12 document that another AMP-dependent enzyme, AMP deaminase (AMPD) is activated in the liver of diabet
14 arliest expressed plant genes and encodes an AMP deaminase (AMPD), which is also an identified herbic
18 d coformycin aglycon analogues with improved AMP deaminase (AMPDA) inhibitory potency are described.
20 been identified as inhibition of the enzyme AMP deaminase (EC 3.5.4.6) following phosphorylation at
23 n of the ribosome protein gene RPS5a and the AMP deaminase gene FAC1, both of which are essential for
26 ata: 1) confirm that available literature on AMP deaminase is likely derived from N-truncated enzymes
32 egradation pathway through the activation of AMP deaminase resulting in uric acid production and the
33 hat disruption of the gene amdA that encodes AMP deaminase results in a significantly increased propo
34 ically up-regulated (lipin, metallothionein, AMP deaminase, RNA helicase-related protein, TG interact
35 a cell-autonomous consequence of the loss of AMP deaminase since mutant cells developed together with
37 ed a decrease in the extractable activity of AMP deaminase that correlates with a strong, noncovalent
38 his finding, we investigated the activity of AMP deaminase, the enzyme that irreversibly deaminates A
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