3.5.4.6: AMP deaminase

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For detailed information about AMP deaminase, go to the full flat file.

Reaction

Synonyms

5'-adenosine monophosphate deaminase, 5'-adenylic acid deaminase, 5-adenylate deaminase, 5-adenylic acid deaminase, 5-AMP aminohydrolase, 5-AMP deaminase, adenosine 5-monophosphate deaminase, adenosine 5-phosphate aminohydrolase, adenosine 5-phosphate deaminase, adenosine monophosphate deaminase, adenosine monophosphate deaminase 3, adenosine monophosphate deaminase-1, adenosine-5'-monophosphate deaminase, adenyl deaminase, adenylate aminohydrolase, adenylate deaminase, adenylate desaminase, adenylic acid deaminase, adenylic deaminase, AMP aminase, AMP deaminase, AMP deaminase 3, AMP deaminase H-type, AMP deaminase isoform E, AMP deaminase type 3, AMP deaminase1, AMP-aminohydrolase, AMP-deaminase, AmpD, AMPD1, AMPD2, AMPD3, AMPDA, deaminase, adenylate, embryonic factor 1, EMBRYONIC FACTOR1, Erythrocyte AMP deaminase, FAC1, Heart-type AMPD, muscle AMP deaminase, Myoadenylate deaminase

ECTree

     3 Hydrolases

         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

             3.5.4 In cyclic amidines

                3.5.4.6 AMP deaminase

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Results	in table
52	Activating Compound
8499	AA Sequence
10	Application
1	CAS Registry Number
10	Cloned(Commentary)
2	Crystallization (Commentary)
1392	Disease/ Diagnostics
4	Expression
11	General Information
10	General Stability
27	IC50 Value
130	Inhibitors
1	Ki Value [mM]
35	KM Value [mM]
2	Localization
25	Metals/Ions
26	Molecular Weight [Da]
11	Natural Substrates/ Products (Substrates)
112	Organism
6	Pathway
36	pH Optimum
7	pH Range
7	pH Stability
2	Posttranslational Modification
6	Protein Variants
43	Purification (Commentary)
2	Reaction
2	Reaction Type
106	Reference
99	Source Tissue
28	Specific Activity [micromol/min/mg]
7	Storage Stability
94	Substrates and Products (Substrate)
19	Subunits
101	Synonyms
1	Systematic Name
6	Temperature Optimum [°C]
2	Temperature Range [°C]
8	Temperature Stability [°C]

Application

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Application on EC 3.5.4.6 - AMP deaminase

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

analysis

Rattus norvegicus

-

assessment of synthetic nitro- and polycyclic musks, imidazolium ionic liquids and N-glucopyranosyl ammonium salts

668434

biotechnology

Yarrowia lipolytica

-

multicopy integrants of crt genes and co-expression of AMP deaminase improve lycopene production in Yarrowia lipolytica. It is possible to make use of the obtained strains to meet the industrial demand of lycopene production on the basis of further genetic and process optimization

757279

food industry

4 entries

medicine

2 entries

synthesis

2 entries

food industry

Aspergillus oryzae

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noting the use of the enzyme from Aspergillus oryzae in food intended for human consumption and potential presence at trace levels in finished goods, a series of safety studies including an in vitro Ames test and chromosome aberration assay with Chinese hamster lung fibroblasts are conducted along with a 90-day oral toxicity study in rats. AMP deaminase shows no evidence of genotoxicity in the in vitro tests. Following gavage administration of Sprague-Dawley rats at dosages of 19.8, 198.4, or 1984 mg total organic solids (TOS)/kg body weight (bw)/day for 90 days, no adverse effects on body weight gain, food consumption, hematology, clinical chemistry, urinalysis, ophthalmological and histopathological examinations are observed. The no-observed-adverse-effect level is considered to be 1984 mg TOS/kg bw/day, the highest dose tested. Results of the genotoxicity studies and subchronic rat study support the safe use of AMP deaminase produced from Aspergillus oryzae in food production

756761

food industry

Aspergillus oryzae

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production of 5'-IMP as food additives and pharmaceutical intermediate, important enzyme for the food industry

756756

food industry

Aspergillus oryzae GX-AD08

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production of 5'-IMP as food additives and pharmaceutical intermediate, important enzyme for the food industry

-

food industry

Aspergillus oryzae DEA262

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noting the use of the enzyme from Aspergillus oryzae in food intended for human consumption and potential presence at trace levels in finished goods, a series of safety studies including an in vitro Ames test and chromosome aberration assay with Chinese hamster lung fibroblasts are conducted along with a 90-day oral toxicity study in rats. AMP deaminase shows no evidence of genotoxicity in the in vitro tests. Following gavage administration of Sprague-Dawley rats at dosages of 19.8, 198.4, or 1984 mg total organic solids (TOS)/kg body weight (bw)/day for 90 days, no adverse effects on body weight gain, food consumption, hematology, clinical chemistry, urinalysis, ophthalmological and histopathological examinations are observed. The no-observed-adverse-effect level is considered to be 1984 mg TOS/kg bw/day, the highest dose tested. Results of the genotoxicity studies and subchronic rat study support the safe use of AMP deaminase produced from Aspergillus oryzae in food production

-

medicine

Mus musculus

-

AMPD3 is a potential candidate for a pharmacological therapeutic strategy for remote reperfusion lung injury

686111

medicine

Homo sapiens

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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

710799

synthesis

Aspergillus oryzae

-

the recombinant enzyme is rapidly inactivated below pH 6.0 and at temperatures above 35 °C but under optimal conditions catalysed the highly efficient transformation of AMP to IMP with minimal by-products, suggesting that it could be used for IMP production following protein engineering

755821

synthesis

Aspergillus oryzae 3811

-

the recombinant enzyme is rapidly inactivated below pH 6.0 and at temperatures above 35 °C but under optimal conditions catalysed the highly efficient transformation of AMP to IMP with minimal by-products, suggesting that it could be used for IMP production following protein engineering

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