Min Fey Chek

Min Fey Chek
Nara Institute of Science and Technology | NAIST

PhD

About

21
Publications
3,236
Reads
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319
Citations
Additional affiliations
October 2017 - March 2021
Nara Institute of Science and Technology
Position
  • Post-doctoral researcher
Education
October 2013 - September 2017
Nara Institute of Science and Technology
Field of study
  • Structural Biology
October 2009 - April 2013
University of Science Malaysia
Field of study
  • Molecular Biology
October 2006 - September 2009
University of Science Malaysia
Field of study
  • Microbiology

Publications

Publications (21)
Article
Full-text available
Polyhydroxyalkanoate (PHA) is a promising candidate for use as an alternative bioplastic to replace petroleum-based plastics. Our understanding of PHA synthase PhaC is poor due to the paucity of available three-dimensional structural information. Here we present a high-resolution crystal structure of the catalytic domain of PhaC from Chromobacteriu...
Article
Full-text available
Polyhydroxyalkanoates (PHAs) are biopolymers synthesized by a wide range of bacteria, which serve as a promising candidate in replacing some conventional petrochemical-based plastics. PHA synthase (PhaC) is the key enzyme in the polymerization of PHA, and the crystal structures were successfully determined using the catalytic domain of PhaC from Cu...
Article
Full-text available
Biodegradable polyester polyhydroxyalkanoate (PHA) is a promising bioplastic material for industrial use as a replacement for petroleum-based plastics. PHA synthase PhaC forms an active dimer to polymerize acyl moieties from the substrate acyl-coenzyme A (CoA) into PHA polymers. Here we present the crystal structure of the catalytic domain of PhaC...
Chapter
The natural polyester polyhydroxyalkanoate (PHA) is synthesized as an energy storage via thioester exchange reaction in microbial cells. The thermal and mechanical properties of PHA can be varied by modifying the monomeric composition, molecular weight, and chemical modification. To date, many efforts have been made to understand the polymerization...
Article
Full-text available
Background Among the polyhydroxyalkanoate (PHA), poly[(R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate] [P(3HB-co-3HHx)] is reported to closely resemble polypropylene and low-density polyethylene. Studies have shown that PHA synthase (PhaC) from mangrove soil (PhaCBP-M-CPF4) is an efficient PhaC for P(3HB-co-3HHx) production and N-termini of PhaCs i...
Article
The Bin-Amphiphysin-Rvs (BAR) domain of endophilin binds to the cell membrane and shapes it into a tubular shape for endocytosis. Endophilin has a Src-homology 3 (SH3) domain at their C-terminal. The SH3 domain interacts with the proline-rich motif (PRM) that is found in proteins such as neural Wiskott-Aldrich syndrome protein (N-WASP). Here, we re...
Article
The higher-order assembly of Bin-amphiphysin-Rvs (BAR) domain proteins, including the FCH-BAR (F-BAR) domain proteins, into lattice on the membrane is essential for the formation of subcellular structures. However, the regulation of their ordered assembly has not been elucidated. Here, we show that the higher ordered assembly of growth-arrested spe...
Article
Ideonella sakaiensis 201-F6 is a bacterium capable of degrading and assimilating poly(ethylene terephthalate) (PET). A recent study revealed its capability in accumulating intracellular polyhydroxyalkanoate (PHA) at high levels using PET as a carbon source. The finding demonstrated that I. sakaiensis can mediate the direct conversion of non-biodegr...
Article
Poly[(R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate] [P(3HB-co-3HHx)] has a high potential to serve as a commercial bioplastic due to its biodegradability, thermoplastic and mechanical properties. The properties of this copolymer are greatly affected by the composition of 3HHx monomer. One of the most efficient ways to modulate the composition of...
Article
Polyhydroxyalkanoates (PHAs) are considered good candidates in replacing commercial petrochemical plastics in certain applications like single-use packaging since they are biodegradable, biocompatible and share similar properties with conventional plastics. PHA synthase (PhaC) is the key enzyme in PHA biosynthesis. There are four classes of PhaC, n...
Article
Full-text available
Glutamine synthetase (GS) is a decameric enzyme that plays a key role in nitrogen metabolism. Acetylation of the N-terminal degron (N-degron) of GS is essential for ubiquitylation and subsequent GS degradation. The full-length GS structure showed that the N-degron is buried inside the GS decamer and is inaccessible to the acetyltransferase. The str...
Article
Polyhydroxyalkanoates (PHAs) are biopolyesters synthesized by microorganisms as intracellular energy reservoirs under stressful environmental conditions. PHA synthase (PhaC) is the key enzyme responsible for PHA biosynthesis, but the importance of its N- and C-terminal ends still remains elusive. Six plasmid constructs expressing truncation variant...
Article
Full-text available
Vesicle amine transport protein-1 (VAT-1) has been implicated in the regulation of vesicular transport, mitochondrial fusion, phospholipid transport and cell migration, and is a potential target of anticancer drugs. Little is known about the molecular function of VAT-1. The amino acid sequence indicates that VAT-1 belongs to the quinone oxidoreduct...
Article
Among the various types of polyhydroxyalkanoate (PHA), poly[(R)-3-hydroxybutyrate-co-(R)-3-hydroxyhexanoate] [P(3HB-co-3HHx)] has a high potential to serve as commercial bioplastic due to its striking resemblance to petroleum-based plastics. In this study, five different genotypes of C. necator transformants harbouring the PhaCBP-M-CPF4 gene (inclu...
Preprint
Full-text available
Biodegradable polyester polyhydroxyalkanoate (PHA) is a promising bioplastic material for industrial use as a replacement for petroleum-based plastics. PHA synthase PhaC forms an active dimer to polymerize acyl moieties from the substrate acyl-coenzyme A (CoA) into PHA polymers. Here we present the crystal structure of the catalytic domain of PhaC...
Poster
Full-text available
PHA synthase (PhaC) is the key enzyme in the polymerization of polyhydroxyalkanoates (PHAs), a biodegradable polymer produced by a wide range of bacteria. Here we report the crystal structure of the catalytic domain of PhaC from Chromobacterium sp. USM2 (PhaCcs‐CAT) at atomic resolution (1.48Å). The crystal structure contains two molecules, which f...

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