4.2.1.112: acetylene hydratase
This is an abbreviated version!
For detailed information about acetylene hydratase, go to the full flat file.
Word Map on EC 4.2.1.112
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4.2.1.112
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pelobacter
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acetylenicus
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tungstoenzyme
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wiv
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nonredox
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bioinspired
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w-containing
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e-4-hydroxy-3-methyl-but-2-enyl
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qm-only
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pterin
- 4.2.1.112
- pelobacter
- acetylenicus
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tungstoenzyme
- wiv
-
nonredox
-
bioinspired
-
w-containing
-
e-4-hydroxy-3-methyl-but-2-enyl
-
qm-only
- pterin
Reaction
Synonyms
(E)-4-hydroxy-3-methyl-but-2-enyl diphosphate reductase, AH, HMBPP reductase, ispH, More, tungsten-dependent acetylene hydratase
ECTree
4.2.1.112 acetylene hydrataseAdvanced search results
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results (Metals Ions
Metals Ions on EC 4.2.1.112 - acetylene hydratase
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METALS and IONS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Fe2+
Iron
Iron-sulfur cluster
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dependent on, the enzyme is a tungsten/iron-sulfur protein, 4.8 mol of iron per mol of enzyme and 3.9 mol od acid-labile sulfur per mol of enzyme
Molybdenum
Tungsten
additional information
Fe2+
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[Fe4S4] cluster involved in hydratase reaction. The enzyme protects the [Fe4S4] cluster from O2 complexed with intermediate or product
Fe2+
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dependent on, the enzyme is a tungsten/iron-sulfur protein with [3Fe-4S], 2.0 gAV, low potential [4Fe-4S] cluster which is highly sensitive to oxidation, 4.8 mol of iron per mol of enzyme, 3.9 mol of acid-labile sulfur per mol of enzyme
Fe2+
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dependent on, the enzyme is a tungsten/iron-sulfur protein with [4Fe-4S], N-terminal binding cluster Cys-Xaa-Cys-Xaa-Cys
Fe2+
in [4Fe-4S] cluster, the enzyme contains 3.7-3.9 mol Fe/mol enzyme
Iron
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non-redox-active tungsten/[4Fe-4S] enzyme, a cubane-type [4Fe:4S] cluster, structure analysis, overview
Iron
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acetylene hydratase is a tungsten, iron-sulfur enzyme, contains 4.8 mol of iron per mol of enzyme
Molybdenum
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a Mo-dependent active form of AH (Mo-AH) can also be obtained from Rhodobacter capsulatus
Molybdenum
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1.3 mol of molybdopterin-guanine dinucleotide per mol of enzyme
Molybdenum
a Mo-dependent active form of AH (Mo-AH) can also be obtained from Pelobacter acetylenicus
Tungsten
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a non-redox-active tungsten/[4Fe-4S] enzyme, contains two molybdopterin guanine dinucleotide cofactors, MGD, designated P and Q, structure analysis, bis-molybdopterin guanine dinucleotide-ligated tungsten atom, overview, the tungsten center binds a water molecule that is activated by an adjacent aspartate residue, enabling to attack acetylene bound in a distinct, hydrophobic pocket, this mechanism requires a strong shift of pKa of the aspartate, caused by nearby low-potential [4Fe:4S] cluster, overview
Tungsten
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dependent on, the enzyme is a tungsten/iron-sulfur protein
Tungsten
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dependent on, the enzyme is a tungsten/iron-sulfur protein, 0.4 mol of tungsten per mol of enzyme
Tungsten
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dependent on, the enzyme is a tungsten/iron-sulfur protein, 0.5 mol of tungsten per mol of enzyme
Tungsten
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acetylene hydratase is a tungsten, iron-sulfur enzyme, active W(IV) state structure, contains 0.4 mol of tungsten per mol of enzymeoverview
Tungsten
bound with two pyranopterins, the enzyme contains 0.4-0.5 mol W/mol enzyme
additional information
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Mo-dependent enzyme is approximately 10fold less active than the native W-dependent enzyme
additional information
the dependence of AH activity on the applied redox potential gives a midpoint potential of -340 mV. Mo-dependent enzyme is approximately 10fold less active than the native W-dependent enzyme. Attempts to insert vanadium into the enzyme's active site fail
additional information
the dependence of AH activity on the applied redox potential gives a midpoint potential of -340 mV. Mo-dependent enzyme is approximately 10fold less active than the native W-dependent enzyme. W is generally preferred over Mo in low-potential redox catalysis
