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
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3.5.4.19
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hi
-
vannielii
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phosphoribosyl-atp
-
methanobacterium
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methanococcus
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metalloenzyme
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purine
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thermoautotrophicum
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drug development
- 3.5.4.19
- hi
- vannielii
-
phosphoribosyl-atp
-
methanobacterium
-
methanococcus
-
metalloenzyme
- purine
- thermoautotrophicum
- drug development
Reaction
Synonyms
HisI, N1-(5'-phosphoribosyl) adenosine-5'-monophosphate cyclohydrolase, phosphoribosyladenosine monophosphate cyclohydrolase, PR-AMP cyclohydrolase, PRA-CH, PRAMP-cyclohydrolase
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Metals Ions
Metals Ions on EC 3.5.4.19 - phosphoribosyl-AMP cyclohydrolase
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Cd2+
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0.95 Cd2+ per enzyme subunit, competes with and replaces Zn2+, binding affects the enzyme structure, three Cd2+ are coordinated by residues Asp85 and Cys86 from one monomer and Cys109 from the other monomer, the fourth Cd2+ is bound by His16 and Asp89
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
Zn2+
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