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3.5.3.1: arginase

This is an abbreviated version!
For detailed information about arginase, go to the full flat file.

Word Map on EC 3.5.3.1

Reaction

L-arginine
+
H2O
=
L-ornithine
+
Urea

Synonyms

ARG, Arg I, Arg II, ARG1, ARG2, ARGAH1, ARGAH2, ArgI, arginase, arginase 1, arginase 1a, arginase 1b, arginase 2a, arginase 2b, arginase I, arginase II, arginase type I, arginase-1, arginase-2, arginase1, arginine amidinase, arginine amidohydrolase-1, arginine amidohydrolase-2, arginine transamidinase, canavanase, human arginase type I, Kidney-type arginase, L-arginase, L-arginine amidino hydrolase, L-arginine amidinohydrolase, L-arginine amidohydrolase, L-arginine ureahydrolase, Liver-type arginase, mitochondrial arginase, More, Non-hepatic arginase, PMN arginase, recombinant human arginase I, rhArg-PEG, rhArg1, RocF, serum arginase, SmARG, tissue arginase, type II arginase

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.3 In linear amidines
                3.5.3.1 arginase

Metals Ions

Metals Ions on EC 3.5.3.1 - arginase

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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cd2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Cu2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Fe
-
cysteine-iron promotes arginase activity
Fe3+
-
the enzyme retains 38.7% of its original activity after dialysis. In the presence of Mn2+ as a cofactor, the enzyme regains 95% of its initial activity
Guanidinium chloride
the single mutant R308A changes to a trimeric and kinetically cooperative form, whereas the other enzyme variants are not altered
Hg2+
chelating loosely bound Mn2+ and replacing it with a variety of bivalent metal ions including Mg2+, Zn2+, Ni2+, Hg2+, Cu2+, Co2+, Ca2+ and Cd2+ retains its enzymatic activity
Magnesium
stabilizes the protein. In the absence of Mg2+, a complete loss of secondary structure is observed for certain elements
Manganese
the more deeply buried Mn2+ ion A is coordinated by residues His193, Asp216, Asp220 and Asp323. The second metal, Mn2+B is co-ordinated by His218, Asp216, Asp323, Asp325
NaCl
the enzyme is optimally active at 100 mM NaCl, but as the salt concentration increase, the activity of the enzyme is reduced to almost half of the maximal activity but the enzyme is still partially active
additional information