Identification and characterization of a novel citrate synthase from <i>Streptomyces diastaticus</i> No. 7 strain M1033

Ge, Yadong; Cao, Zhengyu; Song, Ping; Zhu, Guoping

doi:10.1002/bab.1372

Cited by 12 publications

(6 citation statements)

References 44 publications

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“…In terms of activators, AMP upregulates the activity of CSs from Azotobacter vinelandii 47 and Streptomyces diastaticus No. 7 strain M1033 24 . However, Sy CS was activated by ADP rather than AMP (Fig.…”

Section: Discussionmentioning

confidence: 99%

Citrate synthase from Synechocystis is a distinct class of bacterial citrate synthase

Ito

Koyama

Osanai

2019

Sci Rep

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Citrate synthase (CS, EC 2.3.3.1) catalyses the initial reaction of the tricarboxylic acid (TCA) cycle. Although CSs from heterotrophic bacteria have been extensively studied, cyanobacterial CSs are not well-understood. Cyanobacteria can produce various metabolites from carbon dioxide. Synechocystis sp. PCC 6803 ( Synechocystis 6803) is a cyanobacterium used to synthesize metabolites through metabolic engineering techniques. The production of acetyl-CoA-derived metabolites in Synechocystis 6803 has been widely examined. However, the biochemical mechanisms of reactions involving acetyl-CoA in Synechocystis 6803 are poorly understood. We characterised the CS from Synechocystis 6803 ( Sy CS) and compared its characteristics with other bacterial CSs. Sy CS catalysed only the generation of citrate, and did not catalyse the cleavage of citrate. It is suggested that Sy CS is not related to the reductive TCA cycle. The substrate affinity and turnover number of Sy CS were lower than those of CSs from heterotrophic bacteria. Sy CS was activated by MgCl 2 and CaCl 2 , which inhibit various bacterial CSs. Sy CS was not inhibited by ATP and NADH; which are typical feedback inhibitors of other bacterial CSs. Sy CS was inhibited by phosphoenolpyruvate and activated by ADP, which has not been reported for CSs from heterotrophic bacteria. Thus, Sy CS showed unique characteristics, particularly its sensitivity to effectors.

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Section: Discussionmentioning

confidence: 99%

Citrate synthase from Synechocystis is a distinct class of bacterial citrate synthase

Ito

Koyama

Osanai

2019

Sci Rep

View full text Add to dashboard Cite

show abstract

“…The enzymatic activity of CS was determined at 412 nm with a microplate reader by a previously described method with slight modification . Assays were performed at room temperature in a solution of 10 mM Tris‐HCl buffer (pH 8.0), 0.2 mM acetyl‐CoA, 0.3 mM OAA, and 0.1 mM DTNB in a volume of 100 μL.…”

Section: Methodsmentioning

confidence: 99%

p‐Hydroxybenzyl alcohol inhibits four obesity‐related enzymes in vitro

Choi

Yeo

Kim

et al. 2018

J Biochem & Molecular Tox

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Recently, antiobesity studies using the method of inhibiting enzymatic activity of obesity‐related enzymes as targets have received considerable attention. The aims of the current study were to investigate whether p‐hydroxybenzyl alcohol (HBA), identified from Cudrania tricuspidata fruits with antiobesity effects, inhibits the activity of digestive and obesity‐related enzymes and acts as an inhibitor against four target enzymes in kinetic studies. In vitro enzyme assays showed HBA at the highest concentration significantly reduced the enzymatic activity of four targets: pancreatic lipase (IC50 = 2.34‐3.70 μM), α‐glycosidase (IC50 = 9.08 μM), phosphodiesterase IV (IC50 = 4.99 μM), and citrate synthase (IC50 = 2.07 μM) enzymes. Based on the results of kinetic assays, the types of inhibition were investigated. Our findings indicate that HBA could have antiobesity efficacy, and it deserves further study.

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“…Another conserved amino acid is arginine in the DPR conserved amino acid sequence and aspartic or glutamic acid in the conserved NVD/E. All of these were previously reported as essential residues involved in interactions with the substrate OXA in Streptomyces [15]. All CSs have a common ancestor but are separated into two main lineages.…”

Section: Tca Cyclementioning

confidence: 99%

Multiplicity in the Genes of Carbon Metabolism in Antibiotic-Producing Streptomycetes

Takahashi¹,

Alanís²,

Hernández³

et al. 2022

Actinobacteria - Diversity, Applications and Medical Aspects

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Streptomycetes exhibit genetic multiplicity, like many other microorganisms, and redundancy occurs in many of the genes involved in carbon metabolism. The enzymes of the glycolytic pathway presenting the greatest multiplicity were phosphofructokinase, fructose 1,6-bisphosphate aldolase, glyceraldehyde-3-phosphate dehydrogenase, and pyruvate kinase. The genes that encode citrate synthase and subunits of the succinate dehydrogenase complex are the ones that show the greatest multiplicity, while in the phosphoenolpyruvate-pyruvate-oxaloacetate node, only malic enzymes and pyruvate phosphate dikinase present two copies in some Streptomyces. The extra DNA from these multiple gene copies can be more than 50 kb, and the question arises whether all of these genes are transcribed and translated. As far as we know, there is few information about the transcription of these genes in any of this Streptomyces, nor if any of the activities that are encoded by a single gene could be limiting both for growth and for the formation of precursors of the antibiotics produced by these microorganisms. Therefore, it is important to study the transcription and translation of genes involved in carbon metabolism in antibiotic-producing Streptomyces growing on various sugars.

show abstract

Identification and characterization of a novel citrate synthase from Streptomyces diastaticus No. 7 strain M1033

Cited by 12 publications

References 44 publications

Citrate synthase from Synechocystis is a distinct class of bacterial citrate synthase

Citrate synthase from Synechocystis is a distinct class of bacterial citrate synthase

p‐Hydroxybenzyl alcohol inhibits four obesity‐related enzymes in vitro

Multiplicity in the Genes of Carbon Metabolism in Antibiotic-Producing Streptomycetes

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