1.1.1.23: histidinol dehydrogenase
This is an abbreviated version!
For detailed information about histidinol dehydrogenase, go to the full flat file.
Reaction
Synonyms
11412251, BN980_GECA03s06082g, BsHDH, GcHDH, HDH, HIS4 protein, HisD, histidinol dehydrogenase, HLDase, L-histidinol dehydrogenase
ECTree
1.1.1.23 histidinol dehydrogenaseAdvanced search results
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37903
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Metals Ions
Metals Ions on EC 1.1.1.23 - histidinol dehydrogenase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cd2+
Co2+
Cu2+
Mg2+
Mn2+
Ni2+
Zn2+
additional information
Cd2+
activates, to a higher degree than Zn2+
Mn2+
activates, to a higher degree than Zn2+, which stabilizes the enzyme in its catalytically active form
Mn2+
activates, to a higher degree than Zn2+, which stabilizes the enzyme in its catalytically active form
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
-
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
required, active site-bound, one Zn2+ ion per monomer. The Zn2+ ion plays a crucial role in the proper positioning of the substrate, binding structure, overview
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
required, one Zn2+ bound per subunit of the dimer. Zn2+ ion is octahedrally coordinated to Gln267, His270, Asp369, His428, and two ligands from L-histidinol
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. Binding structure analysis
Zn2+
-
essential for activity, one Zn atom per subunit
Zn2+
metalloenzyme containing one Zn2+ cation in each subunit. His261 and His418 are candidates for zinc ion ligands, as affinities for metal ions decrease with substitutions at these residues. Binding structure analysis
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
-
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
the enzyme is metal-dependent, activity of the apo-enzyme can be rescued by addition of Mn2+, Mg2+, Ca2+, and Zn2+, but not by addition of Cd2+, Co2+ and Ni2+, overview
additional information
-
the enzyme is metal-dependent, activity of the apo-enzyme can be rescued by addition of Mn2+, Mg2+, Ca2+, and Zn2+, but not by addition of Cd2+, Co2+ and Ni2+, overview
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
additional information
the presence of a divalent metal ion is essential for the enzymatic activity: replacement of the Zn2+ cation with Mg2+, Ni2+, Co2+ or Cu2+ causes a decrease of enzymatic activity, while replacement with Mn2+ or Cd2+ enhances the enzyme activity
