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Literature summary for 3.5.4.6 extracted from

  • Bausch-Jurken, M.T.; Sabina, R.L.
    Divergent N-terminal regions in AMP deaminase and isoform-specific catalytic properties of the enzymes (1995), Arch. Biochem. Biophys., 321, 372-380.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ATP activates Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.6 0.8 AMP AMPD1, endogenous, with 12.5 mM ATP Homo sapiens
0.6 1 AMP AMPD1, endogenous, without ATP Homo sapiens
1.1 2.2 AMP AMPD2, endogenous, with 12.5 mM ATP Homo sapiens
1.4
-
AMP recombinant AMPD1, with 12.5 mM ATP Homo sapiens
3.2
-
AMP recombinant AMPD1, without ATP Homo sapiens
3.5
-
AMP recombinant AMPD2, with 12.5 mM ATP Homo sapiens
4.5 9.9 AMP AMPD2, endogenous, without ATP Homo sapiens
11.5
-
AMP recombinant AMPD2, without ATP Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
AMPD1, AMPD2 and AMPD3
-

Purification (Commentary)

Purification (Comment) Organism
expression in Escherichia coli Homo sapiens

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
AMP + H2O
-
Homo sapiens IMP + NH3
-
ir