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Literature summary extracted from

  • Alarcon, R.; Orellana, M.S.; Neira, B.; Uribe, E.; Garcia, J.R.; Carvajal, N.
    Mutational analysis of substrate recognition by human arginase type I -agmatinase activity of the N130D variant (2006), FEBS J., 273, 5625-5631.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.3.1 expressed in Escherichia coli strain JM109 Homo sapiens
3.5.3.11 expressed in Escherichia coli strain JM109 Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.5.3.1 N130D 17% activity compared to the wild type enzyme, the mutant is also active on agmatine, the N130D mutant enzyme is inactive after dialysis against EDTA and assay in the absence of Mn2+ Homo sapiens
3.5.3.1 N130Q after dialysis against EDTA and assay in the absence of Mn2+, the wild type-like N130Q mutant enzyme exhibits 50% activity Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.3.1 EDTA after dialysis against EDTA and assay in the absence of Mn2+, the wild type enzyme exhibits 50% activity Homo sapiens
3.5.3.1 Guanidinium chloride
-
Homo sapiens
3.5.3.1 L-ornithine
-
Homo sapiens
3.5.3.11 putrescine linear competitive inhibitor Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.3.1 1.5
-
L-arginine wild type enzyme, at 37°C Homo sapiens
3.5.3.1 13.3
-
L-arginine mutant enzyme N130D, at 37°C Homo sapiens
3.5.3.11 1.4
-
agmatine
-
Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.3.1 Mn2+ essentiell for activity Homo sapiens
3.5.3.11 Mn2+ totally dependent on Mn2+ for catalytic activity Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.3.1 120000
-
SDS-PAGE Homo sapiens
3.5.3.11 120000
-
SDS-PAGE Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.3.1 L-arginine + H2O Homo sapiens
-
L-ornithine + urea
-
?
3.5.3.1 additional information Homo sapiens the wild type enzyme does not hydrolyze 1-amino-4-guanidinobutane (agmatine) ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.5.3.1 Homo sapiens
-
-
-
3.5.3.11 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.3.1 DEAE-cellulose column chromatography Homo sapiens
3.5.3.11 DEAE-cellulose column chromatography Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.3.11 liver
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.3.1 L-arginine + H2O
-
Homo sapiens L-ornithine + urea
-
?
3.5.3.1 additional information the wild type enzyme does not hydrolyze 1-amino-4-guanidinobutane (agmatine) Homo sapiens ?
-
?
3.5.3.11 agmatine + H2O the N130D mutant of arginase type I is able to cleave not only arginine but also agmatine (1-amino-4-guanidinobutane) Homo sapiens putrescine + urea
-
?

Synonyms

EC Number Synonyms Comment Organism
3.5.3.1 arginase type I
-
Homo sapiens
3.5.3.1 L-arginine amidino hydrolase
-
Homo sapiens
3.5.3.11 N130D variant of arginase type I
-
Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.5.3.1 33
-
L-arginine mutant enzyme N130D, at 37°C Homo sapiens
3.5.3.1 190
-
L-arginine wild type enzyme, at 37°C Homo sapiens
3.5.3.11 3
-
agmatine
-
Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.5.3.1 1
-
L-ornithine wild type enzyme Homo sapiens
3.5.3.1 7.8
-
L-ornithine mutant enzyme N130D Homo sapiens
3.5.3.1 39
-
Guanidinium chloride mutant enzyme N130D Homo sapiens
3.5.3.1 56
-
Guanidinium chloride wild type enzyme Homo sapiens
3.5.3.11 1.3
-
putrescine
-
Homo sapiens