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Literature summary extracted from

  • D'Ordine, R.L.; Linger, R.S.; Thai, C.J.; Davisson, V.J.
    Catalytic zinc site and mechanism of the metalloenzyme PR-AMP cyclohydrolase (2012), Biochemistry, 51, 5791-5803.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
3.5.4.19 C109/C116 no measurable catalytic activity, not capable of binding Zn2+ Methanococcus vannielii
3.5.4.19 C109A no measurable catalytic activity, not capable of binding Zn2+ Methanococcus vannielii
3.5.4.19 C116A no measurable catalytic activity, still capable of binding Zn2+ Methanococcus vannielii
3.5.4.19 C93A no measurable catalytic activity Methanococcus vannielii
3.5.4.19 D92E 180fold loss in catalytic efficiency (kcat/Km), decrease in Zn2+ content Methanococcus vannielii
3.5.4.19 D94A no measurable catalytic activity, decrease in Zn2+ content Methanococcus vannielii
3.5.4.19 D94E 2300fold decrease in activity, decrease in Zn2+ content Methanococcus vannielii
3.5.4.19 H110A 500fold decrease in activity, no decrease in Zn2+ content Methanococcus vannielii

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.5.4.19 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 Methanococcus vannielii
3.5.4.19 methyl methane thiosulfonate compromises the Zn2+ binding properties of the protein inducing loss of up to 90% of the metal Methanococcus vannielii

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.4.19 0.18
-
 1-(5-phospho-beta-D-ribosyl)-AMP mutant enzyme D94E, pH and temperature not specified in the publication Methanococcus vannielii
3.5.4.19 0.83
-
 1-(5-phospho-beta-D-ribosyl)-AMP mutant enzyme H110A, pH and temperature not specified in the publication Methanococcus vannielii
3.5.4.19 2.3
-
 1-(5-phospho-beta-D-ribosyl)-AMP mutant enzyme D92E, pH and temperature not specified in the publication Methanococcus vannielii
3.5.4.19 4 10 1-(5-phospho-beta-D-ribosyl)-AMP wild-type enzyme, pH and temperature not specified in the publication Methanococcus vannielii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.4.19 Mg2+ required for cataltic activity. The C93 reactivity is modulated by the presence of the Zn2+ and Mg2+ and substantiates the role of this residue as a metal ligand Methanococcus vannielii
3.5.4.19 Zn2+ metalloprotein. The Zn2+ coordination site involves the three conserved cysteine residues. The C93 reactivity is modulated by the presence of the Zn2+ and Mg2+ and substantiates the role of this residue as a metal ligand Methanococcus vannielii

Organism

EC Number Organism UniProt Comment Textmining
3.5.4.19 Methanococcus vannielii Q50837
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.4.19 1-(5-phospho-beta-D-ribosyl)-AMP + H2O
-
 Methanococcus vannielii 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.5.4.19 HisI
-
 Methanococcus vannielii
3.5.4.19 N1-(5'-phosphoribosyl) adenosine-5'-monophosphate cyclohydrolase
-
 Methanococcus vannielii
3.5.4.19 PR-AMP cyclohydrolase
-
 Methanococcus vannielii

General Information

EC Number General Information Comment Organism
3.5.4.19 physiological function the enzyme catalyzes the third step of histidine biosynthesis Methanococcus vannielii