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Information on EC 3.5.4.6 - AMP deaminase and Organism(s) Homo sapiens and UniProt Accession Q01433

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EC Tree
     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
IUBMB Comments
cf. EC 3.5.4.17 adenosine-phosphate deaminase.
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This record set is specific for:
Homo sapiens
UNIPROT: Q01433
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
+
=
+
Synonyms
amp deaminase, ampd1, amp-deaminase, adenylate deaminase, ampd2, myoadenylate deaminase, ampd3, adenosine monophosphate deaminase, muscle amp deaminase, ampda, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5'-adenosine monophosphate 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-1
-
-
adenyl deaminase
-
-
-
-
adenylate aminohydrolase
-
-
-
-
adenylate deaminase
-
-
-
-
adenylate desaminase
-
-
-
-
adenylic acid deaminase
-
-
-
-
adenylic deaminase
-
-
-
-
AMP aminase
-
-
-
-
AMP deaminase
-
-
AMP deaminase H-type
-
-
-
-
AMP deaminase isoform E
-
-
AMP-deaminase
-
-
AMPD1
AMPD2
AMPD3
deaminase, adenylate
-
-
-
-
Erythrocyte AMP deaminase
-
-
-
-
Heart-type AMPD
-
-
-
-
Myoadenylate deaminase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidine hydrolysis
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
AMP aminohydrolase
cf. EC 3.5.4.17 adenosine-phosphate deaminase.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-10-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-AMP + H2O
IMP + NH3
show the reaction diagram
-
-
-
-
?
AMP + H2O
IMP + NH3
show the reaction diagram
additional information
?
-
-
key enzyme of nucleotide breakdown is involved in regulation of adenine nucleotide pool in the liver
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
AMP + H2O
IMP + NH3
show the reaction diagram
additional information
?
-
-
key enzyme of nucleotide breakdown is involved in regulation of adenine nucleotide pool in the liver
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
activates erythrocyte AMP deaminase [isoform E (AMPD3)] through a protein-protein interaction between calmodulin and the N-terminal domain of the AMPD3 polypeptide
Cs+
-
activates
K+
-
activates
Li+
-
activates
Na+
-
activates
Rb+
-
activates
Zn2+
-
human muscle AMP-deaminase probably a zinc metalloenzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-bromo-4-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
-
-
2'-AMP
-
in the absence of ATP
2,3-diphosphoglyceric acid
-
ATP counteracts inhibition
3'-AMP
-
in the absence of ATP
3-[2-(3-carboxy-4-bromo-5,6,7,8-tetrahydronaphthyl)ethyl]-3,6,7,8-tetrahydroimidazo[4,5-d][1,3]diazepin-8-ol
-
specific inhibitor
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
-
good inhibitor of isozyme AMPD3
3-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]benzoic acid
-
-
3-[2-(imidazo[2,1-f][1,2,4]triazin-7-yl)ethyl]benzoic acid
-
-
4-[2-(8-hydroxy-7,8-dihydroimidazo[4,5-d][1,3]diazepin-3(6H)-yl)ethyl]-5,6,7,8-tetrahydronaphthalene-2-carboxylic acid
-
-
5'-IMP
-
in the absence of ATP
coformycin 5'-phosphate
-
extremely potent AMPD inhibitor
phosphate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
activates
ATP
-
activates
Ca2+-calmodulin
-
-
-
Calmodulin
-
Ca2+-calmodulin activates erythrocyte AMPD in conditions of disturbed calcium homeostasis during sickle cell disease
dATP
-
activates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6 - 11.5
AMP
additional information
additional information
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0009 - 0.0057
3-[2-(3-carboxy-5,6,7,8-tetrahydronaphthyl)-ethyl]imidazo[2,1-f][1,2,4]triazine
0.1 - 0.37
3-[2-(imidazo[2,1-f][1,2,4]triazin-7-yl)ethyl]benzoic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.008
-
-
0.01
-
enzyme from 40th week-old placenta, in 0.1 M succinate buffer, pH 6.5, at 5 mM substrate (AMP) concentration, at 30°C
0.025
-
enzyme from 33rd week-old placenta, in 0.1 M succinate buffer, pH 6.5, at 5 mM substrate (AMP) concentration, at 30°C
0.037
-
enzyme from 25th week-old placenta, in 0.1 M succinate buffer, pH 6.5, at 5 mM substrate (AMP) concentration, at 30°C
0.077
-
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
125
-
delta M90 AMPD3 mutant
1850
-
wild-type AMPD1
3112
-
DELTA L96 AMPD1 mutant
865
-
wild-type AMPD3
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
-
enzyme from cirrhotic liver
7
-
assay at
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.2
-
pH 6.0: about 55% of maximal activity, pH 7.2: about 55% of maximal activity, normal liver
additional information
-
AMP-deaminase from preterm placenta is less sensitive to pH changes compared to the enzyme from the term organ
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
the expression of AMPD2 gene, extremely weak in mature skeletal muscles of healthy individuals, is also weak in the muscles of Myasthenia gravis patients
Manually annotated by BRENDA team
-
the study fails to confirm a survival benefit among heart failure patients carrying the AMPD1 T-allele (C34T)
Manually annotated by BRENDA team
-
cortex and medulla
Manually annotated by BRENDA team
-
smooth muscle
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AMPD2_HUMAN
879
0
100688
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000 - 400000
-
3 different oligomeric enzyme forms of 140 kDa, 280 kDa, and 400 kDa, gel filtration
145000
-
gel filtration
150000
-
gel filtration
285000
-
sucrose density gradient centrifugation
68000
85000
-
SDS-PAGE
92000
-
SDS-PAGE, 92 and 68 kDa fragments of the enzyme react with specificpolyclonal anti-(human) AMPD2 antibodies
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
-
x * 68000, at least 3 different oligomeric forms of the enzyme, probably dimers, tetramers, and hexamers, SDS-PAGE
tetramer
additional information
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DELTAL96
-
AMPD1 mutant, higher specific activity
DELTAM90
-
AMPD3 mutant, lower specific activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing, unstable
-
sulfhydryl reagents and monovalent cations in high concentrations stabilize
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 4 months, less than 10% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression of AMPD1 and AMPD3 in Sf9 cells
-
native enzyme from human term and preterm placenta
-
partially
-
phosphocellulose column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
expression of AMPD1 and AMPD3 in Sf9 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lian, C.; Harkness, D.R.
The kinetic properties of adenylate deaminase from human erythrocytes
Biochim. Biophys. Acta
341
27-40
1978
Homo sapiens
Manually annotated by BRENDA team
Yun, S.; Suelter, C.H.
Human erythrocyte 5-AMP aminohydrolase. Purification and characterization
J. Biol. Chem.
253
404-408
1978
Homo sapiens
Manually annotated by BRENDA team
Nathans, G.R.; Chang, D.; Deuel, T.F.
AMP deaminase from human erythrocytes
Methods Enzymol.
51
497-502
1979
Homo sapiens
Manually annotated by BRENDA team
Ogasawara, N.; Goto, H.; Yamada, Y.; Watanabe, T.; Asano, T.
AMP deaminase isozymes in human tissues
Biochim. Biophys. Acta
714
298-306
1982
Homo sapiens
Manually annotated by BRENDA team
Stankiewicz, A.
AMP-deaminase from human skeletal muscle. Subunit structure, amino-acid composition and metal content of the homogenous enzyme
Int. J. Biochem.
13
1177-1183
1981
Homo sapiens
Manually annotated by BRENDA team
Kaletha, K.; Nowak, G.
Developmental forms of human skeletal-muscle AMP deaminase. The kinetic and regulatory properties of the enzyme
Biochem. J.
249
255-261
1988
Homo sapiens
Manually annotated by BRENDA team
Mahnke-Zizelman, D.K.; Tullson, P.C.; Sabina, R.L.
Novel aspects of tetramer assembly and N-terminal domain structure and function are revealed by recombinant expression of human AMP deaminase isoforms
J. Biol. Chem.
273
35118-35125
1998
Homo sapiens
Manually annotated by BRENDA team
Bausch-Jurken, M.T.; Sabina, R.L.
Divergent N-terminal regions in AMP deaminase and isoform-specific catalytic properties of the enzymes
Arch. Biochem. Biophys.
321
372-380
1995
Homo sapiens
Manually annotated by BRENDA team
Nowak, G.; Kaletha, K.
Purification and properties of AMP-deaminase from human kidney
Biochem. Med. Metab. Biol.
47
232-241
1992
Homo sapiens
Manually annotated by BRENDA team
Nagel-Starczynowska, G.; Kaletha, K.
AMP-deaminase from human uterine smooth muscle: the effect of DTNB treatment on kinetic and regulatory properties of the enzyme
Biochim. Biophys. Acta
1164
261-267
1993
Homo sapiens
Manually annotated by BRENDA team
Szydlowska, M.; Nagel-Starczynowska, G.; Rybakowska, I.; Swieca, A.; Kaletha, K.
Human liver AMP-deaminase - oligomeric forms of the enzyme
Mol. Cell. Biochem.
241
81-86
2002
Homo sapiens
Manually annotated by BRENDA team
Mahnke, D.K.; Sabina, R.L.
Calcium activates erythrocyte AMP deaminase [isoform E (AMPD3)] through a protein-protein interaction between calmodulin and the N-terminal domain of the AMPD3 polypeptide
Biochemistry
44
5551-5559
2005
Homo sapiens
Manually annotated by BRENDA team
Lucia , L.A.; Martin M. , M.M.; Esteve-Lanao , E.J.; San Juan A. , S.J.; Rubio J. , R.J.; Olivan , O.J.; Arenas , A.J.
C34T mutation of the AMPD1 gene in an elite white runner
Br. J. Sports Med.
40
e7-e7
2006
Homo sapiens
Manually annotated by BRENDA team
Kolek, M.J.; Carlquist, J.F.; Thaneemit-Chen, S.; Lazzeroni, L.C.; Whiting, B.M.; Horne, B.D.; Muhlestein, J.B.; Lavori, P.; Anderson, J.L.
The role of a common adenosine monophosphate deaminase (AMPD)-1 polymorphism in outcomes of ischemic and nonischemic heart failure
J. Card. Fail.
11
677-683
2005
Homo sapiens
Manually annotated by BRENDA team
Dutka, P.; Szydlowska, M.; Chodorowski, Z.; Rybakowska, I.; Nagel-Starczynowska, G.; Kaletha, K.
AMP-deaminase from normal and cirrhotic human liver: a comparative study
Mol. Cell. Biochem.
262
119-126
2004
Homo sapiens
Manually annotated by BRENDA team
Szydlowska, M.; Sledzinski, Z.; Krzyzanowski, M.; Nagel-Starczynowska, G.; Kaletha, K.
Comparative immunologic and kinetic evaluation of AMP-deaminase isolated from normal human liver and hepatocellular carcinoma (HCC)
Nucleosides Nucleotides Nucleic Acids
23
1537-1539
2004
Homo sapiens
Manually annotated by BRENDA team
Sabina, R.L.; Waldenstroem, A.; Ronquist, G.
The contribution of Ca2+ calmodulin activation of human erythrocyte AMP deaminase (isoform E) to the erythrocyte metabolic dysregulation of familial phosphofructokinase deficiency
Haematologica
91
652-655
2006
Homo sapiens
Manually annotated by BRENDA team
Sabbatini, A.R.; Toscano, A.; Aguennouz, M.; Martini, D.; Polizzi, E.; Ranieri-Raggi, M.; Moir, A.J.; Migliorato, A.; Musumeci, O.; Vita, G.; Raggi, A.
Immunohistochemical analysis of human skeletal muscle AMP deaminase deficiency. Evidence of a correlation between the muscle HPRG content and the level of the residual AMP deaminase activity
J. Muscle Res. Cell Motil.
27
83-92
2006
Homo sapiens
Manually annotated by BRENDA team
Roszkowska, A.; Klimek, J.; Kaletha, K.
Expression patterns of AMP-deaminase and cytosolic 5'-nucleotidase genes in human term placenta
Mol. Cell. Biochem.
311
249-251
2008
Homo sapiens
Manually annotated by BRENDA team
Sabina, R.L.; Wandersee, N.J.; Hillery, C.A.
Ca2+-CaM activation of AMP deaminase contributes to adenine nucleotide dysregulation and phosphatidylserine externalization in human sickle erythrocytes
Br. J. Haematol.
144
434-445
2009
Homo sapiens
Manually annotated by BRENDA team
Szydlowska, M.; Roszkowska, A.
Expression patterns of AMP-deaminase isozymes in human hepatocellular carcinoma (HCC)
Mol. Cell. Biochem.
318
1-5
2008
Homo sapiens
Manually annotated by BRENDA team
Borkowski, T.; Orlewska, C.; Slominska, E.M.; Yuen, A.; Lipinski, M.; Rybakowska, I.; Foks, H.; Kaletha, K.K.; Yacoub, M.H.; Smolenski, R.T.
Pharmacological inhibition of AMP-deaminase in rat cardiac myocytes
Nucleosides Nucleotides Nucleic Acids
27
867-871
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Lindell, S.; Maechling, S.; Sabina, R.
Synthesis and biochemical testing of 3-(carboxyphenylethyl)imidazo[2,1-f] [1,2,4]triazines as inhibitors of AMP deaminase
ACS Med. Chem. Lett.
1
286-289
2010
Arabidopsis thaliana, Homo sapiens
Manually annotated by BRENDA team
Taegtmeyer, A.B.; Breen, J.B.; Rogers, P.; Johnson, P.H.; Smith, J.; Smolenski, R.T.; Banner, N.R.; Yacoub, M.H.; Barton, P.J.
Effect of adenosine monophosphate deaminase-1 C34T allele on the requirement for donor inotropic support and on the incidence of early graft dysfunction after cardiac transplantation
Am. J. Cardiol.
103
1457-1462
2009
Homo sapiens
Manually annotated by BRENDA team
Swieca, A.; Rybakowska, I.; Milczarek, R.; Klimek, J.; Kaletha, K.
AMP-deaminase from developing human placenta
Placenta
31
460-462
2010
Homo sapiens
Manually annotated by BRENDA team
Rybakowska, I.; Swieca, A.; Milczarek, R.; Klimek, J.; Kaletha, K.
AMP-deaminase from human preterm placenta - kinetic regulatory properties of enzyme
Placenta
32
704-707
2011
Homo sapiens
Manually annotated by BRENDA team
Rybakowska, I.; Szydlowska, M.; Szrok, S.; Bakula, S.; Kaletha, K.
AMP-deaminase from thymus of patients with myasthenia gravis
Nucleosides Nucleotides Nucleic Acids
34
229-234
2015
Homo sapiens
Manually annotated by BRENDA team
Rybakowska, I.M.; Bakula, S.; Kaletha, K.
Isozymes of AMP-deaminase in muscles Myasthenia Gravis patients
Int. J. Pept. Res. Ther.
22
511-515
2016
Homo sapiens (P23109), Homo sapiens (Q01432), Homo sapiens (Q01433), Homo sapiens
Manually annotated by BRENDA team
Kouzu, H.; Miki, T.; Tanno, M.; Kuno, A.; Yano, T.; Itoh, T.; Sato, T.; Sunaga, D.; Murase, H.; Tobisawa, T.; Ogasawara, M.; Ishikawa, S.; Miura, T.
Excessive degradation of adenine nucleotides by up-regulated AMP deaminase underlies afterload-induced diastolic dysfunction in the type 2 diabetic heart
J. Mol. Cell. Cardiol.
80
136-145
2015
Homo sapiens
Manually annotated by BRENDA team
Joshi, P.R.; Apitz, T.; Zierz, S.
Normal activities of AMP-deaminase and adenylate kinase in patients with McArdle disease
Neurol. Res.
38
1052-1055
2016
Homo sapiens
Manually annotated by BRENDA team