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Polyhydroxyalkanoate synthase (PhaC) : The key enzyme for biopolyester synthesis

Zher Neoh, Soon ; Fey Chek, Min ; Tiang Tan, Hua ; Linares-Pastén, Javier A. LU orcid ; Nandakumar, Ardra ; Hakoshima, Toshio and Sudesh, Kumar (2022) In Current Research in Biotechnology 4. p.87-101
Abstract

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, namely, class I, class II, class III and class IV, each with their distinct characteristics. To date, there are two PhaCs with successfully solved catalytic domain structures. They are PhaC from C. necator (PhaCCn-CAT) (Ser201–Ala589) and PhaC from Chromobacterium sp. USM2 (PhaCCs-CAT) (Phe175–Asn567). Generally, the structure of PhaC consists of... (More)

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, namely, class I, class II, class III and class IV, each with their distinct characteristics. To date, there are two PhaCs with successfully solved catalytic domain structures. They are PhaC from C. necator (PhaCCn-CAT) (Ser201–Ala589) and PhaC from Chromobacterium sp. USM2 (PhaCCs-CAT) (Phe175–Asn567). Generally, the structure of PhaC consists of an N-terminal domain and a C-terminal catalytic domain. The N-terminal domain is flexible and has not been successfully visualized in any existing structures of PhaC. It is suggested to affect the dimerization and stability of the PhaC dimer, enzymatic activity, substrate specificity, molecular weight of PHA produced, expression of PhaC, and its ability to bind to PHA granules and PHA-related proteins. The C-terminal catalytic domain contains the cap subdomain, substrate entrance channel, active site, and product egress tunnel.

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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Catalytic mechanism, N-terminal domain, C-terminal catalytic domain, Polyhydroxyalkanoate, polyhydroxyalkanoate synthase (PhaC) structure
in
Current Research in Biotechnology
volume
4
pages
15 pages
publisher
Elsevier
external identifiers
  • scopus:85123693427
ISSN
2590-2628
DOI
10.1016/j.crbiot.2022.01.002
language
English
LU publication?
yes
additional info
Publisher Copyright: © 2022 The Authors
id
c08ad0b6-a150-48e6-9a0f-75e566795d12
date added to LUP
2022-02-28 08:48:32
date last changed
2023-01-08 20:49:41
@article{c08ad0b6-a150-48e6-9a0f-75e566795d12,
  abstract     = {{<p>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, namely, class I, class II, class III and class IV, each with their distinct characteristics. To date, there are two PhaCs with successfully solved catalytic domain structures. They are PhaC from <i>C. necator</i> (PhaC<sub>Cn</sub>-CAT) (Ser201–Ala589) and PhaC from <i>Chromobacterium</i> sp. USM2 (PhaC<sub>C</sub><sub>s</sub>-CAT) (Phe175–Asn567). Generally, the structure of PhaC consists of an N-terminal domain and a C-terminal catalytic domain. The N-terminal domain is flexible and has not been successfully visualized in any existing structures of PhaC. It is suggested to affect the dimerization and stability of the PhaC dimer, enzymatic activity, substrate specificity, molecular weight of PHA produced, expression of PhaC, and its ability to bind to PHA granules and PHA-related proteins. The C-terminal catalytic domain contains the cap subdomain, substrate entrance channel, active site, and product egress tunnel.</p>}},
  author       = {{Zher Neoh, Soon and Fey Chek, Min and Tiang Tan, Hua and Linares-Pastén, Javier A. and Nandakumar, Ardra and Hakoshima, Toshio and Sudesh, Kumar}},
  issn         = {{2590-2628}},
  keywords     = {{Catalytic mechanism; N-terminal domain, C-terminal catalytic domain; Polyhydroxyalkanoate; polyhydroxyalkanoate synthase (PhaC) structure}},
  language     = {{eng}},
  pages        = {{87--101}},
  publisher    = {{Elsevier}},
  series       = {{Current Research in Biotechnology}},
  title        = {{Polyhydroxyalkanoate synthase (PhaC) : The key enzyme for biopolyester synthesis}},
  url          = {{http://dx.doi.org/10.1016/j.crbiot.2022.01.002}},
  doi          = {{10.1016/j.crbiot.2022.01.002}},
  volume       = {{4}},
  year         = {{2022}},
}