Literature summary for 3.5.1.46 extracted from

Ando, H.; Shigeta, Y.; Baba, T.; Watanabe, C.; Okiyama, Y.; Mochizuki, Y.; Nakano, M.
Hydration effects on enzyme-substrate complex of nylon oligomer hydrolase inter-fragment interaction energy study by the fragment molecular orbital method (2015), Mol. Phys., 113, 319-326 .

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Organism

Organism	UniProt	Comment	Textmining
Paenarthrobacter ureafaciens	P07061	i.e. Flavobacterium sp. K172	-

Synonyms

Synonyms	Comment	Organism
NylB	-	Paenarthrobacter ureafaciens
nylon oligomer hydrolase	-	Paenarthrobacter ureafaciens

General Information

General Information	Comment	Organism
additional information	hydration effects on enzyme-substrate complex of nylon oligomer hydrolase, inter-fragment interaction energy study by the fragment molecular orbital method, overview. Interactions between the substrate, 6-aminohexanoate linear dimer (ALD), and the amino acid residues, such as Asp181, Ser112, and Ile 345, which are regarded as important for enzyme-substrate complex formation by NylB.The direct interaction between ALD and NylB is weakens by hydration, because water molecules cause charge translation or polarisation of ALD or each amino acid residue. But including the interaction energy between ALD and water molecules greatly stabilises this complex. These results indicate the importance of the hydration effects in enzyme-substrate complex formation, quantitative analysis	Paenarthrobacter ureafaciens

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Release 2023.1 (January 2023)