3.5.3.11: agmatinase
This is an abbreviated version!
For detailed information about agmatinase, go to the full flat file.
Word Map on EC 3.5.3.11
-
3.5.3.11
-
putrescine
-
polyamine
-
ornithine
-
imidazoline
-
speb
-
arcaine
-
proclavaminate
-
idazoxan
-
slc7a1
-
efaroxan
- 3.5.3.11
- putrescine
- polyamine
- ornithine
-
imidazoline
- speb
- arcaine
- proclavaminate
-
idazoxan
- slc7a1
-
efaroxan
Reaction
Synonyms
AGM-1, AGMAT, agmatinase, agmatinase-like protein, agmatine ureohydrolase, Alr2310, APL, AUH, HVO_2299, MJ0309, N130D variant of arginase type I, Proclavaminic acid amidino hydrolase, SpeB
ECTree
3.5.3.11 agmatinaseAdvanced search results
results (
results (Metals Ions
Metals Ions on EC 3.5.3.11 - agmatinase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Ca2+
-
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Co2+
-
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Fe2+
Fe(II)-dependent agmatinase. Requires the presence of 4 equivalents of Fe(II) for maximum activity
Mg2+
-
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Mn2+
Zn2+
-
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
Mn2+
-
enzyme loses activity by dialysis against a buffer without cations, but the activity is recovered by the addition of divalent cations. CoCl2 is the most effective, and CaCl2, MnCl2, ZnCl2 or MgCl2 is replaced to some extent instead of CoCl2
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
