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Updated safety evaluation of the food enzyme AMP deaminase from the non‐genetically modified Streptomyces murinus strain AE‐DNTS [PDF]

open access: yesEFSA Journal
The food enzyme AMP deaminase (AMP aminohydrolase; EC 3.5.4.6) is produced with the non‐genetically modified Streptomyces murinus strain AE‐DNTS by Amano Enzyme Inc. In a previous evaluation, the Panel could not conclude on the safety of this food enzyme
EFSA Panel on Food Enzymes (FEZ)   +14 more
doaj   +3 more sources

AMP deaminase 3 deficiency enhanced 5'-AMP induction of hypometabolism. [PDF]

open access: yesPLoS ONE, 2013
A hypometabolic state can be induced in mice by 5'-AMP administration. Previously we proposed that an underlying mechanism for this hypometabolism is linked to reduced erythrocyte oxygen transport function due to 5'-AMP uptake altering the cellular ...
Isadora Susan Daniels   +4 more
doaj   +5 more sources

Safety evaluation of the food enzyme AMP deaminase from the non‐genetically modified Streptomyces murinus strain AE‐DNTS [PDF]

open access: yesEFSA Journal, 2023
The food enzyme AMP deaminase (AMP aminohydrolase; EC 3.5.4.6) is produced with the non‐genetically modified Streptomyces murinus strain AE‐DNTS by Amano Enzyme Inc. The food enzyme is free from viable cells. It is intended to be used in yeast processing
EFSA Panel on Food Contact Materials, Enzymes and Processing Aids (CEP)   +23 more
doaj   +2 more sources

Role of the HPRG Component of Striated Muscle AMP Deaminase in the Stability and Cellular Behaviour of the Enzyme [PDF]

open access: yesBiomolecules, 2018
Multiple muscle-specific isoforms of the Zn2+ metalloenzyme AMP deaminase (AMPD) have been identified based on their biochemical and genetic differences.
Francesca Ronca, Antonio Raggi
doaj   +2 more sources

Effect of isolated AMP deaminase deficiency on skeletal muscle function [PDF]

open access: yesMolecular Genetics and Metabolism Reports, 2014
Mutation of the AMP deaminase 1 (AMPD1) gene, the predominate AMPD gene expressed in skeletal muscle, is one of the most common inherited defects in the Caucasian population; 2–3% of individuals in this ethnic group are homozygous for defects in the ...
Jidong Cheng   +15 more
doaj   +2 more sources

Downregulation of extramitochondrial BCKDH and its uncoupling from AMP deaminase in type 2 diabetic OLETF rat hearts [PDF]

open access: yesPhysiological Reports, 2023
Systemic branched‐chain amino acid (BCAA) metabolism is dysregulated in cardiometabolic diseases. We previously demonstrated that upregulated AMP deaminase 3 (AMPD3) impairs cardiac energetics in a rat model of obese type 2 diabetes, Otsuka Long‐Evans ...
Toshifumi Ogawa   +14 more
doaj   +2 more sources

Muscle AMP deaminase activity was lower in Neandertals than in modern humans [PDF]

open access: yesNature Communications
The enzyme AMPD1 is expressed in skeletal muscle and is involved in ATP production. All available Neandertal genomes carry a lysine-to-isoleucine substitution at position 287 in AMPD1.
Dominik Macak   +6 more
doaj   +2 more sources

Safety evaluation of the food enzyme AMP deaminase from the non‐genetically modified Aspergillus pallidofulvus strain AE‐DN [PDF]

open access: yesEFSA Journal
The food enzyme AMP deaminase (AMP aminohydrolase; EC 3.5.4.6) is produced with the non‐genetically modified Aspergillus pallidofulvus strain AE‐DN by Amano Enzyme Inc. The food enzyme was free from viable cells of the production organism. It is intended
EFSA Panel on Food Enzymes (FEZ)   +17 more
doaj   +2 more sources

Counteracting roles of AMP deaminase and AMP kinase in the development of fatty liver. [PDF]

open access: yesPLoS ONE, 2012
Fatty liver (hepatic steatosis) is associated with nucleotide turnover, loss of ATP and generation of adenosine monophosphate (AMP). It is well known that in fatty liver, activity of the AMP-activated kinase (AMPK) is reduced and that its stimulation can
Miguel A Lanaspa   +13 more
doaj   +2 more sources

Opposing activity changes in AMP deaminase and AMP-activated protein kinase in the hibernating ground squirrel. [PDF]

open access: yesPLoS ONE, 2015
Hibernating animals develop fatty liver when active in summertime and undergo a switch to a fat oxidation state in the winter. We hypothesized that this switch might be determined by AMP and the dominance of opposing effects: metabolism through AMP ...
Miguel A Lanaspa   +17 more
doaj   +2 more sources

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