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3.5.4.19: phosphoribosyl-AMP cyclohydrolase

This is an abbreviated version!
For detailed information about phosphoribosyl-AMP cyclohydrolase, go to the full flat file.

Word Map on EC 3.5.4.19

Reaction

1-(5-phospho-beta-D-ribosyl)-AMP
+
H2O
=
1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide

Synonyms

HisI, N1-(5'-phosphoribosyl) adenosine-5'-monophosphate cyclohydrolase, phosphoribosyladenosine monophosphate cyclohydrolase, PR-AMP cyclohydrolase, PRA-CH, PRAMP-cyclohydrolase

ECTree

     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.4 In cyclic amidines
                3.5.4.19 phosphoribosyl-AMP cyclohydrolase

Inhibitors

Inhibitors on EC 3.5.4.19 - phosphoribosyl-AMP cyclohydrolase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoic acid)
compromises the Zn2+ binding properties of the protein inducing loss of up to 90% of the metal. The enzyme is protected from inactivation by inclusion of the substrate N1-(5'-phosphoribosyl)adenosine 5'-monophosphate, while Mg2+, a metal required for catalytic activity, enhanced the rate of inactivation
EDTA
-
reversible inhibition
methyl methane thiosulfonate
compromises the Zn2+ binding properties of the protein inducing loss of up to 90% of the metal
Zn2+
-
exogenous Zn2+
additional information
ZINC04880153 can be considered as one of the potential lead molecule against HisI drug target in Brucella melitensis. Low binding energy (-9.1kcal/mol) with a molecular weight of 228.191 g/mol. It has 2 H-bond donors and 7 H-bond acceptors. The movement of ZINC04880153 in the binding pockets of HisI shows stability and compact structure with respect to the initial computational model of HisI
-