Substrate Specificity and Allosteric Regulation of a d-Lactate Dehydrogenase from a Unicellular Cyanobacterium are Altered by an Amino Acid Substitution

Abstract Lactate/lactic acid is an important chemical compound for the manufacturing of bioplastics. The unicellular cyanobacterium Synechocystis sp. PCC 6803 can produce lactate from carbon dioxide and possesses d-lactate dehydrogenase (Ddh). Here, we performed a biochemical analysis of the Ddh fro...

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Autores principales:	Shoki Ito, Masahiro Takeya, Takashi Osanai
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/7b3af0d508844558b756b84c780cf633
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spelling	oai:doaj.org-article:7b3af0d508844558b756b84c780cf6332021-12-02T15:05:36ZSubstrate Specificity and Allosteric Regulation of a d-Lactate Dehydrogenase from a Unicellular Cyanobacterium are Altered by an Amino Acid Substitution10.1038/s41598-017-15341-52045-2322https://doaj.org/article/7b3af0d508844558b756b84c780cf6332017-11-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-15341-5https://doaj.org/toc/2045-2322Abstract Lactate/lactic acid is an important chemical compound for the manufacturing of bioplastics. The unicellular cyanobacterium Synechocystis sp. PCC 6803 can produce lactate from carbon dioxide and possesses d-lactate dehydrogenase (Ddh). Here, we performed a biochemical analysis of the Ddh from this cyanobacterium (SyDdh) using recombinant proteins. SyDdh was classified into a cyanobacterial clade similar to those from Gram-negative bacteria, although it was distinct from them. SyDdh can use both pyruvate and oxaloacetate as a substrate and is activated by fructose-1,6-bisphosphate and repressed by divalent cations. An amino acid substitution based on multiple sequence alignment data revealed that the glutamine at position 14 and serine at position 234 are important for the allosteric regulation by Mg2+ and substrate specificity of SyDdh, respectively. These results reveal the characteristic biochemical properties of Ddh in a unicellular cyanobacterium, which are different from those of other bacterial Ddhs.Shoki ItoMasahiro TakeyaTakashi OsanaiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Shoki Ito Masahiro Takeya Takashi Osanai Substrate Specificity and Allosteric Regulation of a d-Lactate Dehydrogenase from a Unicellular Cyanobacterium are Altered by an Amino Acid Substitution
description	Abstract Lactate/lactic acid is an important chemical compound for the manufacturing of bioplastics. The unicellular cyanobacterium Synechocystis sp. PCC 6803 can produce lactate from carbon dioxide and possesses d-lactate dehydrogenase (Ddh). Here, we performed a biochemical analysis of the Ddh from this cyanobacterium (SyDdh) using recombinant proteins. SyDdh was classified into a cyanobacterial clade similar to those from Gram-negative bacteria, although it was distinct from them. SyDdh can use both pyruvate and oxaloacetate as a substrate and is activated by fructose-1,6-bisphosphate and repressed by divalent cations. An amino acid substitution based on multiple sequence alignment data revealed that the glutamine at position 14 and serine at position 234 are important for the allosteric regulation by Mg2+ and substrate specificity of SyDdh, respectively. These results reveal the characteristic biochemical properties of Ddh in a unicellular cyanobacterium, which are different from those of other bacterial Ddhs.
format	article
author	Shoki Ito Masahiro Takeya Takashi Osanai
author_facet	Shoki Ito Masahiro Takeya Takashi Osanai
author_sort	Shoki Ito
title	Substrate Specificity and Allosteric Regulation of a d-Lactate Dehydrogenase from a Unicellular Cyanobacterium are Altered by an Amino Acid Substitution
title_short	Substrate Specificity and Allosteric Regulation of a d-Lactate Dehydrogenase from a Unicellular Cyanobacterium are Altered by an Amino Acid Substitution
title_full	Substrate Specificity and Allosteric Regulation of a d-Lactate Dehydrogenase from a Unicellular Cyanobacterium are Altered by an Amino Acid Substitution
title_fullStr	Substrate Specificity and Allosteric Regulation of a d-Lactate Dehydrogenase from a Unicellular Cyanobacterium are Altered by an Amino Acid Substitution
title_full_unstemmed	Substrate Specificity and Allosteric Regulation of a d-Lactate Dehydrogenase from a Unicellular Cyanobacterium are Altered by an Amino Acid Substitution
title_sort	substrate specificity and allosteric regulation of a d-lactate dehydrogenase from a unicellular cyanobacterium are altered by an amino acid substitution
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/7b3af0d508844558b756b84c780cf633
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Substrate Specificity and Allosteric Regulation of a d-Lactate Dehydrogenase from a Unicellular Cyanobacterium are Altered by an Amino Acid Substitution

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