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Literature summary for 3.5.4.6 extracted from

  • Martini, D.; Ranieri-Raggi, M.; Sabbatini, A.R.; Raggi, A.
    Regulation of skeletal muscle AMP deaminase: lysine residues are critical for the pH-dependent positive homotropic cooperativity behaviour of the rabbit enzyme (2001), Biochim. Biophys. Acta, 1544, 123-132.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ADP wild-type and trinitrobenzene sulfonic acid-desensitized enzyme Oryctolagus cuniculus
native muscle proteinase limited cleavage increases enzyme activity in presence of low concentrations of K+, probably due to removal of a fragment from the enzyme, which holds the enzyme in an inactive state, cleavage occurs e.g. during storage of both the muscle and the purified enzyme Oryctolagus cuniculus
Trypsin limited cleavage increases enzyme activity in presence of low concentrations of K+, probably due to removal of a fragment from the enzyme, which holds the enzyme in an inactive state Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
5,5-dithio-bis(2-nitrobenzoic acid) reaction with thiol groups, leads to a decrease of 20-30% in Vmax Oryctolagus cuniculus
ATP connection between the operation of the hypothesized anionic activating site, responsible for positive homotropic cooperativity, and the inhibition exerted by anionic compounds that compete for the same site, among them ATP is most efficient, no inhibition of the trinitrobenzene sulfonic acid-desensitized enzyme Oryctolagus cuniculus
GTP wild-type and trinitrobenzene sulfonic acid-desensitized enzyme Oryctolagus cuniculus
trinitrobenzene sulfonic acid regulatory function on activity and inhibition by other compounds, e.g. ATP, overview Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics Oryctolagus cuniculus
0.9
-
AMP pH 6.5, 20°C, wild-type enzyme Oryctolagus cuniculus
1
-
AMP pH 6.5, 20°C, trinitrobenzene sulfonic acid-treated enzyme Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
KCl stimulates, no stimulation of the trinitrobenzene sulfonic acid-desensitized enzyme due to blockage of the activation anionic site Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
310000
-
-
Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle from back and hind leg 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
storage of the muscle material as well as the purified enzyme increases the enzyme activity due to limited proteolytic cleavage Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
AMP + H2O
-
Oryctolagus cuniculus IMP + NH3
-
?
additional information 6 lysine residues are critical for the pH-dependent positive homotropic cooperativity behaviour of the enzyme, the lysines form a regulatory anionic site to which AMP must bind to stimulate the enzyme at alkaline pH 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
additional information
-
treatment of the enzyme with trinitrobenzene sulfonic acid at pH 7.2 results in a progressive increase in activity at pH 7.1, no effect on activity at pH 6.5 Oryctolagus cuniculus
6.5
-
-
Oryctolagus cuniculus