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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/11/30 15:18:13」(JST)

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In enzymology, a pyruvate synthase (EC 1.2.7.1) is an enzyme that catalyzes the interconversion of pyruvate and acetyl-CoA. It is also called pyruvate:ferredoxin oxidoreductase (PFOR).

The relevant equilibrium catalysed by PFOR is:

pyruvate + CoA + oxidized ferredoxin acetyl-CoA + CO₂ + reduced ferredoxin + 2 H⁺

The 3 substrates of this enzyme are pyruvate, CoA, and oxidized ferredoxin, whereas its 4 products are acetyl-CoA, CO₂, reduced ferredoxin, and H⁺.

Function

This enzyme participates in 4 metabolic pathways: pyruvate metabolism, propanoate metabolism, butanoate metabolism, and reductive carboxylate cycle (CO₂ fixation).

Its major role is the extraction of reducing equivalents by the decarboxylation. In aerobic organisms, this conversion is catalysed by pyruvate dehydrogenase, also uses thiamine pyrophosphate but relies on lipoate as the electron acceptor. Unlike the aerobic enzyme complex PFOR transfers reducing equivalents to flavins or iron-sulflur clusters. This process links glycolysis to the Wood–Ljungdahl pathway.

Nomenclature

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is pyruvate:ferredoxin 2-oxidoreductase (CoA-acetylating). Other names in common use include:

pyruvate oxidoreductase,
pyruvate synthetase,
pyruvate:ferredoxin oxidoreductase, and
pyruvic-ferredoxin oxidoreductase.

Inhibitors

Amixicile is a potent inhibitor of pyruvate ferredoxin oxidoreductase and is in pre-clinical studies to treat infections of Helicobacter pylori and Clostridium difficile.^[1]

References

^ Warren CA, van Opstal E, Ballard TE, Kennedy A, Wang X, Riggins M, Olekhnovich I, Warthan M, Kolling GL, Guerrant RL, Macdonald TL, Hoffman PS (August 2012). "Amixicile, a novel inhibitor of pyruvate: ferredoxin oxidoreductase, shows efficacy against Clostridium difficile in a mouse infection model". Antimicrob. Agents Chemother. 56 (8): 4103–11. doi:10.1128/AAC.00360-12. PMC 3421617. PMID 22585229.

UpToDate Contents

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English Journal

Functional analysis of differentially expressed proteins in Chinese bayberry (Myrica rubra Sieb. et Zucc.) fruits during ripening.

Chen YY1, Zhang ZH2, Zhong CY3, Song XM3, Lin QH2, Huang CM3, Huang RH3, Chen W4.
Food chemistry.Food Chem.2016 Jan 1;190:763-70. doi: 10.1016/j.foodchem.2015.06.023. Epub 2015 Jun 10.
This study developed a proteome reference map of Myrica rubra fruits at the green, pink and red stages during ripening using two-dimensional gel electrophoresis (2-DE). Forty-six differentially expressed proteins were detected in the gel, of which 43 were successfully identified by matrix-assisted l
PMID 26213036

Hydroxybenzaldoximes Are D-GAP-Competitive Inhibitors of E. coli 1-Deoxy-D-Xylulose-5-Phosphate Synthase.

Bartee D1, Morris F1,2, Al-Khouja A1, Freel Meyers CL3.
Chembiochem : a European journal of chemical biology.Chembiochem.2015 Aug 17;16(12):1771-81. doi: 10.1002/cbic.201500119. Epub 2015 Jul 15.
1-Deoxy-D-xylulose 5-phosphate (DXP) synthase is the first enzyme in the methylerythritol phosphate pathway to essential isoprenoids in pathogenic bacteria and apicomplexan parasites. In bacterial pathogens, DXP lies at a metabolic branch point, serving also as a precursor in the biosynthesis of vit
PMID 26174207

Adaptive mutations in sugar metabolism restore growth on glucose in a pyruvate decarboxylase negative yeast strain.

Zhang Y1,2, Liu G3,4, Engqvist MK5,6, Krivoruchko A7,8, Hallström BM9, Chen Y10,11, Siewers V12,13, Nielsen J14,15,16.
Microbial cell factories.Microb Cell Fact.2015 Aug 8;14(1):116.
BACKGROUND: A Saccharomyces cerevisiae strain carrying deletions in all three pyruvate decarboxylase (PDC) genes (also called Pdc negative yeast) represents a non-ethanol producing platform strain for the production of pyruvate derived biochemicals. However, it cannot grow on glucose as the sole car
PMID 26253003

Japanese Journal

A pyruvate carbon flux tugging strategy for increasing 2,3-butanediol production and reducing ethanol subgeneration in the yeast Saccharomyces cerevisiae

Ishii Jun,Morita Keisuke,Ida Kengo,Kato Hiroko,Kinoshita Shohei,Hataya Shoko,Shimizu Hiroshi,Kondo Akihiko,Matsuda Fumio
Biotechnology for Biofuels (11), 180, 2018-06-26
… Here, we propose a yeast metabolic engineering strategy for decreasing ethanol subgeneration involving tugging the carbon flux at an important hub branching point (e.g., pyruvate). … We validated this possibility by testing 2,3-butanediol (2,3-BDO) production, which is routed via pyruvate as the important hub compound. …
NAID 120006489889

Metabolome analysis-based design and engineering of a metabolic pathway in Corynebacterium glutamicum to match rates of simultaneous utilization of D-glucose and L-arabinose

Kawaguchi Hideo,Yoshihara Kumiko,Hara Kiyotaka Y.,Hasunuma Tomohisa,Ogino Chiaki,Kondo Akihiko
Microbial Cell Factories (17), 76, 2018-05-17
… Metabolome analysis revealed that phosphofructokinase and pyruvate kinase were major bottlenecks for D-glucose and L-arabinose metabolism, respectively. … Based on the results of metabolome analysis, a metabolic pathway was engineered by overexpressing pyruvate kinase in combination with deletion of araR, which encodes a repressor of L-arabinose uptake and catabolism. …
NAID 120006473640

Characterization of Mitochondrial Content and Respiratory Capacities of Broiler Chicken Skeletal Muscles with Different Muscle Fiber Compositions

Hakamata Yuki,Watanabe Kouichi,Amo Taku,Toyomizu Masaaki,Kikusato Motoi
日本家禽学会誌 55(3), 210-216, 2018
… Citrate synthase (CS) activity was the highest in type IIA muscle tissues and isolated mitochondria, among the muscle tissues tested. … Mitochondria from type I muscle exhibited a higher coupled respiration rate induced by pyruvate/malate, palmitoyl-CoA/malate, and palmitoyl-carnitine, as respiratory substrates, than type IIB-muscle mitochondria, while the response of mitochondria from type IIA muscle to those substrates was comparable to that of mitochondria from type I muscle. …
NAID 130007419002

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pyruvate synthase
Identifiers
EC number	1.2.7.1
CAS number	9082-51-3
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
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PMC	articles
PubMed	articles
NCBI	proteins