Structure and function of the N-terminal domain of Ralstonia eutropha polyhydroxyalkanoate synthase, and the proposed structure and mechanisms of the whole enzyme-Reference-Cited by-同舟云学术

Structure and function of the N-terminal domain of Ralstonia eutropha polyhydroxyalkanoate synthase, and the proposed structure and mechanisms of the whole enzyme

Published:2016-11-30 Issue:1 Volume:12 Page:1600649
ISSN:1860-6768
Container-title:Biotechnology Journal
language:en
Short-container-title:Biotechnol. J.

Author:

Kim Yeo-Jin¹,Choi So Young²,Kim Jieun¹,Jin Kyeong Sik³,Lee Sang Yup²,Kim Kyung-Jin¹

Affiliation:

1. School of Life Sciences, KNU Creative BioResearch Group; Kyungpook National University; Daegu Republic of Korea

2. Metabolic and Biomolecular Engineering National Research Laboratory, Department of Chemical and Biomolecular Engineering (BK21 Plus Program), BioProcess Engineering Research Center, Center for Systems and Synthetic Biotechnology, and Institute for the BioCentury; Korea Advanced Institute of Science and Technology (KAIST); Daejeon Republic of Korea

3. Pohang Accelerator Laboratory; Pohang University of Science and Technology; Pohang Republic of Korea

Funder

Ministry of Science, ICT and Future Planning

Publisher

Wiley

Subject

Molecular Medicine,Applied Microbiology and Biotechnology,General Medicine

Reference36 articles.

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4. Poly-β-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC);Peoples;J. Biol. Chem.,1989

5. PHA synthase activity controls the molecular weight and polydispersity of polyhydroxybutyrate in vivo;Sim;Nat. Biotechnol.,1997

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