Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.3.18 extracted from

  • Bogumil, R.; Knipp, M.; Fundel, S.M.; Vasak, M.
    Characterization of dimethylargininase from bovine brain: evidence for a zinc binding site (1998), Biochemistry, 37, 4791-4798.
    View publication on PubMed
Search for more literature for 3.5.3.18

General Stability

General Stability Organism
Zn2+ has a structure-stabilizing role Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
Zn2+ besides the tightly bound zinc, additional Zn2+ inhibit competitively Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.31
-
 NG,NG-dimethyl-L-arginine
-
 Bos taurus
1.6
-
 NG-monomethyl-L-arginine
-
 Bos taurus

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ contains one tightly bound zinc ion Bos taurus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
NG,NG-dimethyl-L-arginine + H2O Bos taurus enzyme is involved in regulation of the levels of the natural occuring free arginine derivatives L-Nomega,Nomega-dimethylarginine and L-Nomega-methylarginine, which are reversible inhibitors of nitric oxide synthase dimethylamine + L-citrulline
-
 ?

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
NG,NG-dimethyl-L-arginine + H2O
-
 Bos taurus dimethylamine + L-citrulline
-
 ?
NG,NG-dimethyl-L-arginine + H2O enzyme is involved in regulation of the levels of the natural occuring free arginine derivatives L-Nomega,Nomega-dimethylarginine and L-Nomega-methylarginine, which are reversible inhibitors of nitric oxide synthase Bos taurus dimethylamine + L-citrulline
-
 ?
NG-monomethyl-L-arginine + H2O
-
 Bos taurus citrulline + methylamine
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 2 h, holo-enzyme retains ca. 56% of the original activity, no residual activity of the apoenzyme. Thermal denaturation of both protein forms is irreversible Bos taurus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.27
-
 NG,NG-dimethyl-L-arginine
-
 Bos taurus
0.34
-
 NG-monomethyl-L-arginine
-
 Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2
-
 hydrolysis of NG,NG-dimethyl-L-arginine Bos taurus