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Literature summary for 3.5.4.6 extracted from

  • Ranieri-Raggi, M.; Martini, D.; Sabbatini, A.R.; Moir, A.J.; Raggi, A.
    Isolation by zinc-affinity chromatography of the histidine-proline-rich-glycoprotein molecule associated with rabbit skeletal muscle AMP deaminase. Evidence that the formation of a protein-protein complex between the catalytic subunit and the novel component is critical for the stability of the enzyme (2003), Biochim. Biophys. Acta, 1645, 81-88.
    View publication on PubMed
Search for more literature for 3.5.4.6

General Stability

General Stability Organism
EDTA stabilizes the purified enzyme during storage Oryctolagus cuniculus
enzyme is associated to the histidine-proline-rich-glycoprotein HPRG via its catalytic subunit in a protein-protein complex, which is critical for the enzyme stability Oryctolagus cuniculus
additional information Oryctolagus cuniculus
phosphate stabilizes the tetrameric structure of the enzyme Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
phosphate competitive inhibitor, stabilizing the tetrameric enzyme structure Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.4
-
 AMP crude enzyme extract, pH 6.5, 20°C Oryctolagus cuniculus
0.6
-
 AMP imidazole-eluted purified enzyme, pH 6.5, 20°C Oryctolagus cuniculus
1
-
 AMP EDTA-eluted purified enzyme, pH 6.5, 20°C Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
K+ stabilizing the enzyme structure Oryctolagus cuniculus
Zn2+ enzyme HPRG component binds to Zn2+ Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
80000
-
 4 * 80000, stabilized by phosphate Oryctolagus cuniculus
309000
-
-
 Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein enzyme contains a histidine-proline-rich-glycoprotein HPRG component Oryctolagus cuniculus

Purification (Commentary)

Purification (Comment) Organism
both native enzyme and its histidine-proline-rich-glycoprotein HPRG component, the latter being completely separated from the enzyme and its catalytic subunit by Zn2+-affinity chromatography including presence of 1 M KCl Oryctolagus cuniculus

Reaction

Reaction Comment Organism Reaction ID
AMP + H2O = IMP + NH3 enzyme is associated to the histidine-proline-rich-glycoprotein HPRG via its catalytic subunit in a protein-protein complex Oryctolagus cuniculus
a

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1100
-
 purified enzyme Oryctolagus cuniculus

Storage Stability

Storage Stability Organism
4°C, purified enzyme, loss of 50% activity within 1 week in absence of EDTA, in presence of EDTA it is stable for 10 days, fragmentation occurs at 4°C Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
AMP + H2O
-
 Oryctolagus cuniculus IMP + NH3
-
 ?

Subunits

Subunits Comment Organism
? x * 70000-95000, histidine-proline-rich-glycoprotein HPRG component, partially proteolyzed or deglycosylated, SDS-PAGE Oryctolagus cuniculus
More enzyme contains a histidine-proline-rich-glycoprotein HPRG component, bound via its catalytic subunit in a protein-protein complex, which is critical for the enzyme stability, disulfide bridges are involved in formation of enzyme conformation Oryctolagus cuniculus
tetramer 4 * 80000, stabilized by phosphate Oryctolagus cuniculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
 assay at Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5
-
-
 Oryctolagus cuniculus