Purification and properties of a citrate synthase from Nitrosomonas sp. TK794 and a comparison with the enzymes of another nitrifying bacteria

Asai, Tomohide; Takahashi, Reiji; Fujioka, Tomoko; Tokuyama, Tatsuaki

doi:10.1016/0922-338x(95)92747-z

Cited by 4 publications

(4 citation statements)

References 22 publications

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“…Na + , Ca 2+ , and Mg 2+ could stimulate enzyme activity slightly which was in contrast to the report that CS activity was strongly inhibited by these ions in eukaryotic cells . On the other hand, the effects of Mg 2+ and Mn 2+ on Sd CS activity were different from which on Ne CS . The enzyme activity was strongly inhibited by Ag + , Pb 2+ , Hg 2+ , and Zn 2+ , and was slightly inhibited by Ni 2+ , Co 2+ , and Cu 2+ , which is similar compared with Ne CS .…”

Section: Discussioncontrasting

confidence: 80%

“…On the other hand, the effects of Mg 2+ and Mn 2+ on Sd CS activity were different from which on Ne CS . The enzyme activity was strongly inhibited by Ag + , Pb 2+ , Hg 2+ , and Zn 2+ , and was slightly inhibited by Ni 2+ , Co 2+ , and Cu 2+ , which is similar compared with Ne CS .…”

Section: Discussionmentioning

confidence: 76%

“…The effect of pH on Sd CS is similar compared with CSs from Streptomyces hygroscopicus ( Sh CS) (pH 8.0–8.5) , Nitrosomonas sp. TK794 ( Ns CS) (pH 7.5–8.0) , Geobacter sulfurreducens ( Gs CS) (pH 8.0) , and the eukaryote Hemicentrotus pulcherrimus ( Hp CS) (pH 7.8) . Moreover, Sd CS activity was optimal at approximately 35 °C (Fig.…”

Section: Discussionmentioning

confidence: 97%

“…It was reported that monovalent or divalent cations activated or inhibited CS activity in some bacteria or eukaryotic cells . For example, the CS from Nitrosomonas europaea ( Ne CS) was strongly inhibited by Ag + , Cu 2+ , Zn 2+ , and Hg 2+ at the concentration of 0.1 mM and was enhanced by K + at the concentration of 0.1–100 mM, whereas Mg 2+ and Mn 2+ were found to have no effect on the enzyme . The CS from sea urchin eggs was inhibited by both monovalent (50 mM) and divalent (10 mM) cations ( e .…”

Section: Discussionmentioning

confidence: 99%

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

Cao

Song

et al. 2015

Biotech and App Biochem

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Citrate synthase (CS) is a key enzyme of the tricarboxylic acid cycle and is widely distributed among prokaryotes and eukaryotes. Here, we report for the first time, the cloning, expression, and characterization of a novel CS from Streptomyces diastaticus No. 7 strain M1033 (SdCS). Gel filtration chromatography and matrix-assisted laser-desorption ionization-time-of-flight mass spectrometry (MALDI-TOF-MS) analyses indicate that SdCS forms homodimers with a molecular mass of approximately 100.0 kDa. The predicted amino acid sequence of SdCS is highly similar to those of bacterial homodimeric type I CSs. The pH and temperature optima for SdCS activity were 8.0 and 35 °C, respectively. The half-life (t1/2 ) of SdCS was 10 Min at 50 °C and was increased to 210 Min in the presence of oxaloacetate. The kinetic parameters of SdCS (kcat = 262.8 and 230.7 s(-1); Km = 58.4 and 11.2 µM for acetyl-CoA and oxaloacetate, respectively) were comparable to those of dimeric CSs isolated from Gram-positive bacteria and eukaryotes. Moreover, SdCS activity was inhibited by ATP and ADP and stimulated by AMP. These findings provide a foundation for further investigations on the three-dimensional structure and mechanism of catalysis of SdCS.

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Section: Discussioncontrasting

confidence: 80%

Section: Discussionmentioning

confidence: 76%