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
-
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 (Engineering
Engineering on EC 4.2.1.112 - acetylene hydratase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D13A
site-directed mutagenesis of catalytically important Asp13, a direct neighbor of the [4Fe-4S] coordinating Cys12, forms a close hydrogen bond of 2.41 A to the oxygen ligand of the W ion, the mutant shows significant loss of activity compared to wild-type
D13E
I142A
K48A
D13E
Syntrophotalea acetylenica WoAcy1 / DSM 3246
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site-directed mutagenesis, almost inactive mutant
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I142A
Syntrophotalea acetylenica WoAcy1 / DSM 3246
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site-directed mutagenesis, the mutant shows a marked loss of activity compared to the wild-type enzyme
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K48A
Syntrophotalea acetylenica WoAcy1 / DSM 3246
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
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additional information
D13E
site-directed mutagenesis of catalytically important Asp13, a direct neighbor of the [4Fe-4S] coordinating Cys12, forms a close hydrogen bond of 2.41 A to the oxygen ligand of the W ion, the mutant shows unaltered activity compared to wild-type
I142A
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site-directed mutagenesis, the mutant shows a marked loss of activity compared to the wild-type enzyme
I142A
site-directed mutagenesis, Ile142 is part of the hydrophobic ring that is proposed to form the substrate binding cavity at the end of the access tunnel towards the active site, its exchange against alanine results in a strong loss of activity
K48A
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site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme
K48A
site-directed mutagenesis of the residue involved in electron transfer between the two cofactors, the exchange of Lys48 against alanine does not affect catalysis
additional information
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construction of active-site variants, and of a fusion protein of the N-terminal chaperone binding site of the Escherichia coli nitrate reductase NarG to the AH gene improving the yield and activity of AH and its variants significantly, overview
additional information
Syntrophotalea acetylenica WoAcy1 / DSM 3246
-
construction of active-site variants, and of a fusion protein of the N-terminal chaperone binding site of the Escherichia coli nitrate reductase NarG to the AH gene improving the yield and activity of AH and its variants significantly, overview
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