Polyester synthases: natural catalysts for plastics (Record no. 49581)

MARC details
000 -LEADER
fixed length control field 02948nam a2200241Ia 4500
003 - CONTROL NUMBER IDENTIFIER
control field MX-MdCICY
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250625160132.0
040 ## - CATALOGING SOURCE
Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-15400
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 250602s9999 xx |||||s2 |||| ||und|d
245 10 - TITLE STATEMENT
Title Polyester synthases: natural catalysts for plastics
490 0# - SERIES STATEMENT
Volume/sequential designation BioChemical Journal, 376(1), p.15-33, 2003
520 3# - SUMMARY, ETC.
Summary, etc. Polyhydroxyalkanoates (PHAs)are biopolyesters composed of hydroxy fatty acids, which represent a complex class of storage polyesters. They are synthesized by a wide range of different Gram-positive and Gram-negative bacteria, as well as by some Archaea, and are deposited as insoluble cytoplasmic inclusions. Polyester synthases are the key enzymes of polyester biosynthesis and catalyse the conversion of (R)-hydroxyacyl-CoA thioesters to polyesters with the concomitant release of CoA. These soluble enzymes turn into amphipathic enzymes upon covalent catalysis of polyester-chain formation. A self-assembly process is initiated resulting in the formation of insoluble cytoplasmic inclusions with a phospholipid monolayer and covalently attached polyester synthases at the surface. Surface-attached polyester synthases show a marked increase in enzyme activity. These polyester synthases have only recently been biochemically characterized. An overview of these recent ?ndings is provided. At present, 59 polyester synthase structural genes from 45 different bacteria have been cloned and the nucleotide sequences have been obtained. The multiple alignment of the primary structures of these polyester synthases show an overall identity of 8-96 per cent with only eight strictly conserved amino acid residues. Polyester synthases can been assigned to four classes based on their substrate specificity and subunit composition. The current knowledge on the organization of the polyester synthase genes, and other genes encoding proteins related to PHA metabolism, is compiled. In addition, the primary structures of the 59 PHA synthases are aligned and analysed with respect to highly conserved amino acids, and biochemical features of polyester synthases are described. The proposed catalytic mechanism based on similarities to a/ß-hydrolases and mutational analysis is discussed. Different threading algorithms suggest that polyester synthases belong to the a/ß-hydrolase superfamily, with a conserved cysteine residue as catalytic nucleophile. This review provides a survey of the known biochemical features of these unique enzymes and their proposed catalytic mechanism.
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element BIOPOLYESTER
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element BIOPOLYMER
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element CATALYTIC MECHANISM
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element POLYESTER SYNTHASE
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element POLYHYDROXYALKANOATE (PHA)
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PHA SYNTHASE.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Rehm, B.H.A.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/1PzZ6r14NJIjCGEpFfbA2D6jdidNFP8L8/view?usp=drivesdk">https://drive.google.com/file/d/1PzZ6r14NJIjCGEpFfbA2D6jdidNFP8L8/view?usp=drivesdk</a>
Public note Para ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Source of classification or shelving scheme Clasificación local
Koha item type Documentos solicitados
Holdings
Lost status Source of classification or shelving scheme Damaged status Not for loan Collection Home library Current library Shelving location Date acquired Total checkouts Full call number Date last seen Price effective from Koha item type
  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-15400 25.06.2025 25.06.2025 Documentos solicitados