188.8.131.52 - Agmatinase
- Agmatine ureohydrolase.
gmatine + H2O = putrescine + urea
There are no Cofactors for this Enzyme
There are no Reaction Mechanism for this Enzyme
Organism KM Value [mM] Substrate Comment Methanocaldococcus jannaschii 0.00069 agmatine pH 7.5, 70°C, mutant enzyme C71S
There are no reaction parameters information for this Enzyme.
Organism pH Range Comment Methanocaldococcus jannaschii 6.5 - 10 no activity is detected at pH 6.5 and the measured activity steadily increases to pH 10.0. Higher pH values are tested but the observation of activity is dependent on the buffer used and are not reported here. Agmatine shows no hydrolysis in the pH 10 and 11 buffers and assay conditions used Pyrococcus horikoshii 9.5 - 12.5 pH 9.5: about 50% of maximal activity, pH 12.5: about 85% of maximal activity
- Adeno-Associated Virus-Mediated Knockdown of Agmatinase Attenuates Inflammation and Tumorigenesis in a Mouse Model of Colitis-Associated Colorectal Cancer.
- Putrescine Biosynthesis from Agmatine by Arginase (TtARG) in Thermus thermophilus.
- The expression of agmatinase manipulates the affective state of rats subjected to chronic restraint stress.
- Neuroprotection by agmatine: Possible involvement of the gut microbiome?
- Guanidino acid hydrolysis by the human enzyme annotated as agmatinase.
- Metabolites, gene expression, and gut microbiota profiles suggest the putative mechanisms via which dietary creatine increases the serum taurine and g-ABA contents in Megalobrama amblycephala.
- The effects of a comparatively higher dose of 1000 mg/kg/d of oral L- or D-arginine on the L-arginine metabolic pathways in male Sprague-Dawley rats.
- Compartmentation of Putrescine Synthesis in Plants
- Metabolites, gene expression and gut microbiota profiles suggest the putative mechanisms via which dietary creatine increases the serum taurine and g- ABA contents in Megalobrama amblycephala
- Urea and ocular surface: Synthesis, secretion and its role in tear film homeostasis.
- New Insights into the Determinants of Specificity in Human Type I Arginase: Generation of a Mutant That Is Only Active with Agmatine as Substrate.