Improvement of Aminopeptidase Activity of Dizinc(II) Complexes by Increasing Substrate Accessibility | Zendy

Md. Jamil Hossain | Zendy; Akinobu Wada | Zendy; Yasuhiro Igarashi | Zendy; Kei-ichiro Aimono | Zendy; Keisuke Suzuki | Zendy; Katsuya Tone | Zendy; Hiroshi Sakiyama | Zendy

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Improvement of Aminopeptidase Activity of Dizinc(II) Complexes by Increasing Substrate Accessibility

Author(s) -

Md. Jamil Hossain,

Akinobu Wada,

Yasuhiro Igarashi,

Kei-ichiro Aimono,

Keisuke Suzuki,

Katsuya Tone,

Hiroshi Sakiyama

Publication year - 2011

Publication title -

international journal of inorganic chemistry

Language(s) - English

Resource type - Journals

eISSN - 2090-2026

pISSN - 2090-2034

DOI - 10.1155/2011/395418

Subject(s) - hydrolysis , chemistry , aminopeptidase , substrate (aquarium) , stereochemistry , leucine , organic chemistry , biochemistry , amino acid , biology , ecology

A new dizinc(II) complex, [Zn2(bhmp)(MeCO2)2]BPh4 [(bhmp)−: 2,6-bis[bis(2-hydroxyethyl)aminomethyl]-4-methylphenolate anion], performs aminopeptidase activity to hydrolyze L-leucine-p-nitroanilide. As compared with a related dizinc(II) complex [Zn2(bomp)(MeCO2)2]BPh4 [(bomp)−: 2,6-bis[bis(2-methoxyethyl)aminomethyl]-4-methylphenolate anion], the activity of the present bhmp complex was about 80 times greater than that of the bomp complex. This is mainly because the substrate accessibility was improved by changing the terminal methoxy groups to hydroxyl groups

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