Reaction participants Show >> << Hide
-
Name help_outline
(6-hydroxyhexanoyl)n
Identifier
CHEBI:195201
Charge
-1
Formula
(C6H10O2)n.HO
Search links
Involved in 1 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
-
Identifier: RHEA-COMP:18659Polymer name: (6-hydroxyhexanoyl)(n)Polymerization index help_outline nFormula HO(C6H10O2)nCharge (-1)(0)nMol File for the polymer
-
Identifier: RHEA-COMP:18660Polymer name: (6-hydroxyhexanoyl)(n−1)Polymerization index help_outline n-1Formula HO(C6H10O2)n-1Charge (-1)(0)n-1Mol File for the polymer
-
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,485 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 6-hydroxyhexanoate Identifier CHEBI:32383 (Beilstein: 3661830; CAS: 1191-25-9) help_outline Charge -1 Formula C6H11O3 InChIKeyhelp_outline IWHLYPDWHHPVAA-UHFFFAOYSA-M SMILEShelp_outline OCCCCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:75967 | RHEA:75968 | RHEA:75969 | RHEA:75970 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
Publications
-
An extracellular lipase from Amycolatopsis mediterannei is a cutinase with plastic degrading activity.
Tan Y., Henehan G.T., Kinsella G.K., Ryan B.J.
An extracellular lipase from <i>Amycolatopsis mediteranei</i> (AML) with potential applications in process biotechnology was recently cloned and examined in this laboratory. In the present study, the 3D structure of AML was elucidated by comparative modelling. AML lacked the 'lid' structure observ ... >> More
An extracellular lipase from <i>Amycolatopsis mediteranei</i> (AML) with potential applications in process biotechnology was recently cloned and examined in this laboratory. In the present study, the 3D structure of AML was elucidated by comparative modelling. AML lacked the 'lid' structure observed in most true lipases and shared similarities with plastic degrading enzymes. Modelling and substrate specificity studies showed that AML was a cutinase with a relatively exposed active site and specificity for medium chain fatty acyl moieties. AML rapidly hydrolysed the aliphatic plastics poly(ε-caprolactone) and poly(1,4-butylene succinate) extended with 1,6-diisocyanatohexane under mild conditions. These plastics are known to be slow to degrade in landfill. Poly(L-lactic acid) was not hydrolysed by AML, nor was the aromatic plastic Polyethylene Terephthalate (PET). The specificity of AML is partly explained by active site topology and analysis reveals that minor changes in the active site region can have large effects on substrate preference. These findings show that extracellular <i>Amycolatopsis</i> enzymes are capable of degrading a wider range of plastics than is generally recognised. The potential for application of AML in the bioremediation of plastics is discussed. << Less
Comput. Struct. Biotechnol. J. 19:869-879(2021) [PubMed] [EuropePMC]