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Literature summary extracted from

  • Quinones, M.; Cofre, J.; Benitez, J.; Garcia, D.; Romero, N.; Gonzalez, A.; Carvajal, N.; Garcia, M.; Lopez, V.; Schenk, G.; Uribe, E.
    Insight on the interaction of an agmatinase-like protein with Mn(2+) activator ions (2015), J. Inorg. Biochem., 145, 65-69 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.3.11 expression in Escherichia coli Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
3.5.3.11 H127A Km-value for agmatine is 2.3fold lower than the Km-value for the wild-type enzyme. kcat is 1.7fold higher as compared to the wild-type enzyme Rattus norvegicus
3.5.3.11 H206A Km-value for agmatine is 2.1fold lower than the Km-value for the wild-type enzyme. kcat is 90% compared to the wild-type value Rattus norvegicus
3.5.3.11 H394A Km-value for agmatine is 2.3fold higher than the Km-value for the wild-type enzyme. kcat ist identical to wild-type enzyme Rattus norvegicus
3.5.3.11 H435A Km-value for agmatine is 1.5fold higher than the Km-value for the wild-type enzyme. kcat ist 70% compared to the wild-type value Rattus norvegicus
3.5.3.11 H65A incubation of the mutant with 50 mM EDTA (pH 7.5) and subsequent dialysis to remove the chelating agent results in the loss of agmatinase activity. Even in the presence of Mn2+ only about 20% of the activity of the mutant enzyme is recovered. Km-value for agmatine is 1.44fold higher than the Km-value for the wild-type enzyme. kcat is 1.1fold higher as compared to the wild-type enzyme Rattus norvegicus

General Stability

EC Number General Stability Organism
3.5.3.11 the enzyme appears to be active in the mono and binuclear form, with binding of the second metal ion increasing both reactivity and stability Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.3.11 EDTA incubation with 50 mM EDTA (pH 7.5) and subsequent dialysis to remove the chelating agent results in the loss of agmatinase activity Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.3.11 1.1
-
 agmatine mutant enzyme H127A, pH 9.0, 37°C Rattus norvegicus
3.5.3.11 1.1
-
 agmatine mutant enzyme H394A, pH 9.0, 37°C Rattus norvegicus
3.5.3.11 1.2
-
 agmatine mutant enzyme H206A, pH 9.0, 37°C Rattus norvegicus
3.5.3.11 1.7
-
 agmatine mutant enzyme H435A, pH 9.0, 37°C Rattus norvegicus
3.5.3.11 2.5
-
 agmatine wild-type enzyme, pH 9.0, 37°C Rattus norvegicus
3.5.3.11 3.6
-
 agmatine mutant enzyme H65A, pH 9.0, 37°C Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.3.11 Mn2+ the enzyme contains one Mn2+ per subunit after purification. Adding extra Mn2+ leads to a further increase in activity. Incubation in the presence of Mn2+ at 60 °C for up to 20 min results in a significant activation in all ALP variants. The activation of the H206A and H435A mutants is comparable to wild-type enzyme (about 4fold increase), while for the remaining mutants (H65A, H127A, H394A) the increase is less significant. His206 is likely to interact with a Mn2+ bound to a high affinity site. His65 and possibly His435 are important for binding of a secondMn2+ to a lower affinity site Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.3.11 agmatine + H2O Rattus norvegicus
-
 putrescine + urea
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.3.11 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.3.11 brain
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.3.11 agmatine + H2O
-
 Rattus norvegicus putrescine + urea
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.3.11 agmatinase-like protein
-
 Rattus norvegicus
3.5.3.11 APL
-
 Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.3.11 0.7
-
 agmatine mutant enzyme H435A, pH 9.0, 37°C Rattus norvegicus
3.5.3.11 0.9
-
 agmatine mutant enzyme H206A, pH 9.0, 37°C Rattus norvegicus
3.5.3.11 1
-
 agmatine mutant enzyme H394A, pH 9.0, 37°C Rattus norvegicus
3.5.3.11 1
-
 agmatine wild-type enzyme, pH 9.0, 37°C Rattus norvegicus
3.5.3.11 1.1
-
 agmatine mutant enzyme H65A, pH 9.0, 37°C Rattus norvegicus
3.5.3.11 1.7
-
 agmatine mutant enzyme H127A, pH 9.0, 37°C Rattus norvegicus