3.5.1.117: 6-aminohexanoate-oligomer endohydrolase
This is an abbreviated version!
For detailed information about 6-aminohexanoate-oligomer endohydrolase, go to the full flat file.
Word Map on EC 3.5.1.117
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3.5.1.117
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arthrobacter
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nylon-6
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flavobacterium
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6-aminohexanoate-dimer
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sitting-drop
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heterodimers
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vapour-diffusion
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amide
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unnatural
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compendium
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man-made
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orthorhombic
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byproduct
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tetramer
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agromyces
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hepes
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doughnut-shaped
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gel-filtration
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industry
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synthesis
- 3.5.1.117
- arthrobacter
- nylon-6
- flavobacterium
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6-aminohexanoate-dimer
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sitting-drop
- heterodimers
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vapour-diffusion
- amide
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unnatural
-
compendium
-
man-made
-
orthorhombic
-
byproduct
- tetramer
- agromyces
- hepes
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doughnut-shaped
-
gel-filtration
- industry
- synthesis
Reaction
Synonyms
6-aminohexanoate oligomer hydrolase, 6-aminohexanoate-dimer hydrolase, 6-aminohexanoate-hydrolase, 6-aminohexanoate-linear-dimer hydrolase, 6-aminohexanoate-oligomer hydrolase, 6-aminohexanoate-oligomer-hydrolase, 6-aminohexanoic acid-oligomer hydrolase, Ahx endo-type-oligomer hydrolase, Ahx oligomer hydrolase, Ahx-linear-dimer hydrolase, Ahx-oligomer hydrolase, AL2 hydrolase, Ald hydrolase, EII, endo-type 6-aminohexanoate oligomer hydrolase, endotype Ahx-oligomer hydrolase, NylB, NylB-type nylon-oligomer hydrolase, NylC, nylon hydrolase, nylon oligomer hydrolase, nylon oligomer-hydrolyzing enzyme, nylon-oligomer hydrolase, nylonase
ECTree
3.5.1.117 6-aminohexanoate-oligomer endohydrolaseAdvanced search results
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results (Engineering
Engineering on EC 3.5.1.117 - 6-aminohexanoate-oligomer endohydrolase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D122G
mutation increases the melting temperature by 24°C compared to wild-type enzyme
D122G/H130Y
mutation increases the melting temperature by 29°C compared to wild-type enzyme
D122G/H130Y/D36A
mutation increases the melting temperature by 32°C compared to wild-type enzyme
D122G/H130Y/D36A/E236Q
mutation increases the melting temperature by 36°C compared to wild-type enzyme
D122G/H130Y/D36A/E263Q
D122G/H130Y/E263Q
mutation increases the melting temperature by 32°C compared to wild-type enzyme
D122G/H130Y/L137A
mutation increases the melting temperature by 2°C compared to wild-type enzyme
G111S
mutation decreases the melting temperature by 9°C compared to wild-type enzyme
G111S/D122G/H130Y
mutation increases the melting temperature by 26°C compared to wild-type enzyme
G111S/D122G/H130Y/L137A
mutation decreases the melting temperature by 1°C compared to wild-type enzyme
H130Y
mutation increases the melting temperature by 11°C compared to wild-type enzyme
L137A
mutation decreases the melting temperature by 11°C compared to wild-type enzyme
D122G
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mutation increases the melting temperature by 24°C compared to wild-type enzyme
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D122G/H130Y/D36A/E263Q
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mutations enhance the protein thermostability by 36°C (melting temperature: 88°C). More than 90% of the enzyme activity is retained after incubation of the mutant for 30 min at 70°C
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G111S
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mutation decreases the melting temperature by 9°C compared to wild-type enzyme
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H130Y
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mutation increases the melting temperature by 11°C compared to wild-type enzyme
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L137A
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mutation decreases the melting temperature by 11°C compared to wild-type enzyme
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Y170F
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site-directed mutagenesis, the Tyr170 is replaced by phenylalanine, which is unable to form a hydrogen bond with the amide bond, thus, resulting in an increase in the activation barrier of more than 10 kcal/mol, but despite the lack of hydrogen bonding between the Y170F and the substrate, the highest free energy barrier for the induced-fit is similar to that of wild-type suggesting that in the induced-fit process, kinetics is little affected by the mutation, hybrid quantum mechanics/molecular mechanics (QM/MM) dynamical simulations
Y170F
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site-directed mutagenesis, the Tyr170 is replaced by phenylalanine, which is unable to form a hydrogen bond with the amide bond, thus, resulting in an increase in the activation barrier of more than 10 kcal/mol, but despite the lack of hydrogen bonding between the Y170F and the substrate, the highest free energy barrier for the induced-fit is similar to that of wild-type suggesting that in the induced-fit process, kinetics is little affected by the mutation, hybrid quantum mechanics/molecular mechanics (QM/MM) dynamical simulations
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D122G/H130Y/D36A/E263Q
mutations enhance the protein thermostability by 36°C (melting temperature: 88°C). More than 90% of the enzyme activity is retained after incubation of the mutant for 30 min at 70°C
D122G/H130Y/D36A/E263Q
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site-directed mutagenesis, the mutant enzyme hydrolyzes polymeric nylon-6 powder, but the extent of the degradation is low
