Cyanophycin and its biosynthesis: not hot but very cool
Covering: 1878 to early 2023 Cyanophycin is a biopolymer consisting of a poly-aspartate backbone with arginines linked to each Asp sidechain through isopeptide bonds. Cyanophycin is made by cyanophycin synthetase 1 or 2 through ATP-dependent polymerization of Asp and Arg, or β-Asp-Arg, respectively....
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| Published in | Natural product reports Vol. 4; no. 9; pp. 1479 - 1497 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
England
Royal Society of Chemistry
20.09.2023
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| Subjects | |
| Online Access | Get full text |
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| Summary: | Covering: 1878 to early 2023
Cyanophycin is a biopolymer consisting of a poly-aspartate backbone with arginines linked to each Asp sidechain through isopeptide bonds. Cyanophycin is made by cyanophycin synthetase 1 or 2 through ATP-dependent polymerization of Asp and Arg, or β-Asp-Arg, respectively. It is degraded into dipeptides by exo-cyanophycinases, and these dipeptides are hydrolyzed into free amino acids by general or dedicated isodipeptidase enzymes. When synthesized, chains of cyanophycin coalesce into large, inert, membrane-less granules. Although discovered in cyanobacteria, cyanophycin is made by species throughout the bacterial kingdom, and cyanophycin metabolism provides advantages for toxic bloom forming algae and some human pathogens. Some bacteria have developed dedicated schemes for cyanophycin accumulation and use, which include fine temporal and spatial regulation. Cyanophycin has also been heterologously produced in a variety of host organisms to a remarkable level, over 50% of the host's dry mass, and has potential for a variety of green industrial applications. In this review, we summarize the progression of cyanophycin research, with an emphasis on recent structural studies of enzymes in the cyanophycin biosynthetic pathway. These include several unexpected revelations that show cyanophycin synthetase to be a very cool, multi-functional macromolecular machine.
Cyanophycin is a widespread natural biopolymer with promising green chemistry applications that is made by an elegant, multifunctional biosynthetic machine. |
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| Bibliography: | Itai Sharon performed undergraduate studies in biology and chemistry at Tel-Aviv University, Israel, and will soon receive his Ph.D. in Biochemistry from McGill University, Canada. His Ph.D. research has focused on the structural and functional characterization of all steps of cyanophycin metabolism, using cryo-electron microscopy, X-ray crystallography, biochemistry and microbiology. Donald Hilvert received a PhD in Chemistry from Columbia University, New York. After postdoctoral studies at Rockefeller University, New York, he joined the faculty of the Scripps Research Institute at La Jolla, California, where he pursued his interests in chemical biology. In 1997 he moved to his current position as Professor of Chemistry at the ETH Zurich. His research program aims to understand the origins of enzyme catalysis, mimic and expand upon these properties, and engineer protein compartments for diverse applications. Martin Schmeing performed graduate research with Tom Steitz at Yale University, studying the architecture and mechanism of the large ribosomal subunit. He then undertook postdoctoral training at the LMB, Cambridge, with Venki Ramakrishnan, using cryo-EM and X-ray crystallography to investigate initiation and elongation of translation. Martin established his laboratory at McGill University in 2010, where he studies nonribosomal peptide synthetases and other macromolecular biosynthetic machines. Martin is currently a James McGill Professor in the Department of Biochemistry and the Director of the McGill Centre de recherche en biologie structurale. ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 |
| ISSN: | 0265-0568 1460-4752 |
| DOI: | 10.1039/d2np00092j |