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Information on EC 3.5.4.6 - AMP deaminase and Organism(s) Gallus gallus

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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:
Gallus gallus
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Word Map
The taxonomic range for the selected organisms is: Gallus gallus
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-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
-
-
-
-
adenyl deaminase
-
-
-
-
adenylate aminohydrolase
-
-
-
-
adenylate deaminase
-
-
-
-
adenylate desaminase
-
-
-
-
adenylic acid deaminase
-
-
-
-
adenylic deaminase
-
-
-
-
AMP aminase
-
-
-
-
AMP deaminase H-type
-
-
-
-
deaminase, adenylate
-
-
-
-
Erythrocyte AMP deaminase
-
-
-
-
Heart-type AMPD
-
-
-
-
muscle AMP deaminase
-
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
AMP + H2O
IMP + NH3
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
metalloenzyme. The metal binding protein histidine-proline-rich glycoprotein (HPRG) participates in the assembly and maintenance of skeletal muscle AMP deaminase (AMPD1) by acting as a zinc chaperone. Based on the preferential localization of HPRG at the sarcomeric I-band and on the presence of a Zn2+ binding motif in the N-terminal regions of fast TnT and of the AMPD1 catalytic subunit, it is hypothesized that the Zn binding properties of HPRG could promote the association of AMPD1 to the thin filament
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
-
above 0.5 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
-
1 mM, activates
ATP
-
1 mM, activates
phosphate
-
0.5 mM, slight activation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
activity of adenosine monophosphate deaminase is significantly higher in chicken of the fast-growing type than in the slow-growing French "Label Rouge" type, and in heavy line typ
Manually annotated by BRENDA team
-
skeletal muscle
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme appears to play a role in regulation of relative concentrations of intracellular purine nucleotide pools, the stabilization of adenylate energy charge, and the deamination of amino acids via the purine nucleotide cycle
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AMPD1_CHICK
26
0
3195
Swiss-Prot
other Location (Reliability: 4)
F1P0N2_CHICK
707
0
81334
TrEMBL
other Location (Reliability: 3)
A0A3Q3AXW9_CHICK
911
0
104407
TrEMBL
other Location (Reliability: 4)
F1NG97_CHICK
765
0
88931
TrEMBL
other Location (Reliability: 2)
A0A3Q2TW68_CHICK
888
0
101826
TrEMBL
other Location (Reliability: 4)
A0A1D5P970_CHICK
941
0
106611
TrEMBL
other Location (Reliability: 1)
A0A860G8M5_CHICK
721
0
83213
TrEMBL
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
276000
-
sucrose density gradient centrifugation
37000
-
x * 37000, SDS-PAGE
69000
-
4 * 69000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 37000, SDS-PAGE
tetramer
-
4 * 69000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 4
-
at high concentrations, 10 days
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4°C or -20°C for up to 10 days, 30 mg/ml protein
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawamura, Y.
Purification and regulatory properties of AMP deaminase from chicken erythrocytes
J. Biochem.
72
21-28
1972
Gallus gallus
Manually annotated by BRENDA team
Kruckeberg, W.C.; Lemley, S.; Chilson, O.P.
Purification, subunit structure, and amino acid composition of avian erythrocyte adenosine monophosphate deaminase
Biochemistry
17
4376-4383
1978
Gallus gallus
Manually annotated by BRENDA team
Kaletha, K.
Regulatory properties of 14-day embryo and adult hen skeletal muscle AMP-deaminase. The influence of pH on the enzyme activity
Biochim. Biophys. Acta
784
90-92
1984
Gallus gallus
Manually annotated by BRENDA team
Swieca, A.; Rybakowska, I.; Koryziak, A.; Klimek, J.; Kaletha, K.
AMP-deaminase from hen stomach smooth muscle - physico-chemical properties of the enzyme
Acta Biochim. Pol.
51
213-218
2004
Gallus gallus
Manually annotated by BRENDA team
El Rammouz, R.; Berri, C.; Le Bihan-Duval, E.; Babile, R.; Fernandez, X.
Breed differences in the biochemical determinism of ultimate pH in breast muscles of broiler chickens--a key role of AMP deaminase?
Poult. Sci.
83
1445-1451
2004
Gallus gallus
Manually annotated by BRENDA team
Ronca, F.; Raggi, A.
Role of the HPRG component of striated muscle AMP deaminase in the stability and cellular behaviour of the enzyme
Biomolecules
8
E79
2018
Rattus norvegicus (P10759), Oryctolagus cuniculus (P81072), Gallus gallus (P81073)
Manually annotated by BRENDA team