Protein Variants | Comment | Organism |
---|---|---|
D15G | site-directed mutagenesis | Arthrobacter sp. |
D181G | site-directed mutagenesis | Arthrobacter sp. |
G181D/H266N | site-directed mutagenesis | Arthrobacter sp. |
G181D/H266N/D370Y | site-directed mutagenesis | Arthrobacter sp. |
P4R | site-directed mutagenesis | Arthrobacter sp. |
S8Q | site-directed mutagenesis | Arthrobacter sp. |
T3A | site-directed mutagenesis | Arthrobacter sp. |
T5S | site-directed mutagenesis | Arthrobacter sp. |
Y170F | 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 | Arthrobacter sp. |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
[N-(6-aminohexanoyl)]n + H2O | Arthrobacter sp. | - |
[N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x | - |
? | |
[N-(6-aminohexanoyl)]n + H2O | Arthrobacter sp. KI72 | - |
[N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arthrobacter sp. | - |
- |
- |
Arthrobacter sp. KI72 | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
[N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x | the Tyr170 residue points the NH group towards the proton-acceptor site of an artificial amide bond, reaction mechanism, overview | Arthrobacter sp. |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nylon-6 polymer + H2O | - |
Arthrobacter sp. | ? | - |
? | |
nylon-6 polymer + H2O | - |
Arthrobacter sp. KI72 | ? | - |
? | |
[N-(6-aminohexanoyl)]n + H2O | - |
Arthrobacter sp. | [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x | - |
? | |
[N-(6-aminohexanoyl)]n + H2O | - |
Arthrobacter sp. KI72 | [N-(6-aminohexanoyl)]n-x + [N-(6-aminohexanoyl)]x | - |
? |
Synonyms | Comment | Organism |
---|---|---|
NylB | - |
Arthrobacter sp. |
nylon oligomer hydrolase | - |
Arthrobacter sp. |
General Information | Comment | Organism |
---|---|---|
evolution | NylB belongs to the class C of the beta-lactamase family, which is characterized by the presence of a catalytic triad, namely, Ser, Tyr, and Lys, having the ability to promote the hydrolysis of amide and/or ester bonds. Natural selection is responsible for the development of the peculiar hydrolytic activity of Arthrobacter sp. KI72 | Arthrobacter sp. |
additional information | the enzyme can adopt two different conformations: a substrate-free form (open form) and a substrate-bound form (closed from), hybrid quantum mechanics/molecular mechanics (QM/MM) dynamical simulations complemented with free energy sampling methods, allow to determine the reaction mechanismin NylB and address one of the possible roles of Tyr170 during the acylation process, enzyme structure and induced-fit process, detailed overview | Arthrobacter sp. |