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AMP deaminase

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(Redirected from Myoadenylate deaminase) Mammalian protein found in Homo sapiens
AMPD1
Identifiers
AliasesAMPD1, MAD, MADA, MMDD, adenosine monophosphate deaminase 1, AMP deaminase, AMPD
External IDsOMIM: 102770; MGI: 88015; HomoloGene: 20; GeneCards: AMPD1; OMA:AMPD1 - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)
Chromosome 1 (human)Genomic location for AMPD1Genomic location for AMPD1
Band1p13.2Start114,673,090 bp
End114,695,618 bp
Gene location (Mouse)
Chromosome 3 (mouse)
Chr.Chromosome 3 (mouse)
Chromosome 3 (mouse)Genomic location for AMPD1Genomic location for AMPD1
Band3 F2.2|3 45.25 cMStart102,981,330 bp
End103,007,036 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • triceps brachii muscle

  • vastus lateralis muscle

  • Skeletal muscle tissue of rectus abdominis

  • biceps brachii

  • glutes

  • Skeletal muscle tissue of biceps brachii

  • muscle of thigh

  • thoracic diaphragm

  • deltoid muscle

  • gastrocnemius muscle
Top expressed in
  • quadriceps femoris muscle

  • muscle of thigh

  • skeletal muscle tissue

  • zone of skin

  • esophagus

  • lip

  • thymus

  • embryo

  • zygote

  • blastocyst
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

270

229665

Ensembl

ENSG00000116748

ENSMUSG00000070385

UniProt

P23109

Q3V1D3

RefSeq (mRNA)

NM_001172626
NM_000036

NM_001033303

RefSeq (protein)

NP_000027
NP_001166097

NP_001028475

Location (UCSC)Chr 1: 114.67 – 114.7 MbChr 3: 102.98 – 103.01 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

AMP deaminase 1 is an enzyme that in humans is encoded by the AMPD1 gene.

Adenosine monophosphate deaminase is an enzyme that converts adenosine monophosphate (AMP) to inosine monophosphate (IMP), freeing an ammonia molecule in the process.

Function

Adenosine monophosphate deaminase 1 catalyzes the deamination of AMP to IMP in skeletal muscle and plays an important role in the purine nucleotide cycle. Two other genes have been identified, AMPD2 and AMPD3, for the liver- and erythrocyte-specific isoforms, respectively. Deficiency of the muscle-specific enzyme is apparently a common cause of exercise-induced myopathy and probably the most common cause of metabolic myopathy in the human.

A research report shows that the widely prescribed diabetes medication metformin works on AMP-activated kinase (AMPK) by directly inhibiting AMP deaminase, thereby increasing cellular AMP.

Regulation

It has been shown that in environments with high potassium concentrations, AMP-deaminase is regulated by ATP and ADP through a “Km-type” mechanism. In low potassium ion concentrations, a mixed “Km V-type” of the regulation is observed.

Pathology

AMPD1 deficiency, also known as myoadenylate deaminase deficiency, is a disorder in which the body produces insufficient AMP deaminase.

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000116748Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000070385Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Mahnke-Zizelman DK, Sabina RL (October 1992). "Cloning of human AMP deaminase isoform E cDNAs. Evidence for a third AMPD gene exhibiting alternatively spliced 5'-exons". J. Biol. Chem. 267 (29): 20866–77. doi:10.1016/S0021-9258(19)36768-7. PMID 1400401.
  6. ^ EntrezGene 270
  7. Ouyang J, Parakhia RA, Ochs RS (January 2011). "Metformin activates AMP kinase through inhibition of AMP deaminase". J. Biol. Chem. 286 (1): 1–11. doi:10.1074/jbc.M110.121806. PMC 3012963. PMID 21059655.
  8. Skladanowski, Andrzej (1979). "Potassium-dependent regulation by ATP and ADP of AMP-deaminase from beef heart". International Journal of Biochemistry. 10 (2): 177–181. doi:10.1016/0020-711X(79)90114-9. PMID 428625.

Further reading

External links

Purine metabolism
Anabolism
R5PIMP:
IMP→AMP:
IMP→GMP:
Nucleotide salvage
Catabolism
Pyrimidine metabolism
Anabolism
Catabolism
Deoxyribonucleotides
Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides /
Amidohydrolases
3.5.2: Cyclic amides/
Amidohydrolases
3.5.3: Linear amidines/
Ureohydrolases
3.5.4: Cyclic amidines/
Aminohydrolases
3.5.5: Nitriles/
Aminohydrolases
3.5.99: Other
Enzymes
Activity
Regulation
Classification
Kinetics
Types
Portal:


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