A novel cold-adapted esterase from Salinisphaera sp. P7-4: Gene cloning, overproduction, and characterization

Kim, Young‐Ok; Park, In-Suk; Kim, Hyung-Kwou; Nam, Bo‐Hye; Kong, Hee Jeong; Kim, Woo Jin; Kim, Dong-Gyun; Kim, Kyung-Kil; Lee, Sang-Jun

doi:10.2323/jgam.57.357

Cited by 10 publications

(8 citation statements)

References 30 publications

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“…A serine hydrolase from Salinisphaera sp . P7‐4 is inhibited by several +2 metal cations, including Co, Ni, Zn, Cu 29 and a serine hydrolase from Photobacterium sp . MA1‐3 is inhibited by several +2 metal cations, including Zn and Cu 30 .…”

Section: Resultsmentioning

confidence: 99%

“…As part of these previous studies, a metal dependence to the thermal stability of Rv0045c was noted with decreasing thermal stability dependent on increasing divalent metal concentrations 22 . A variety of serine hydrolases show metal dependent inhibition of enzymatic activity but the mechanisms for metal‐dependent inhibition have not been investigated further 28–30 . Herein, we measured the divalent metal inhibition profile of Rv0045c and found it to be inhibited by divalent metals with an Irving‐Williams series dependent profile.…”

Section: Introductionmentioning

confidence: 80%

“…22 A variety of serine hydrolases show metal dependent inhibition of enzymatic activity but the mechanisms for metal-dependent inhibition have not been investigated further. [28][29][30] Herein, we measured the divalent metal inhibition profile of Rv0045c and found it to be inhibited by divalent metals with an Irving-Williams series dependent profile. Through the combination of structural analysis with and without zinc and targeted mutagenesis, we traced this metal-dependent inhibition to multiple chelating residues on a flexible loop, suggesting dynamic allosteric regulation of Rv0045c by divalent metals.…”

Section: Introductionmentioning

confidence: 98%

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Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C

et al. 2021

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Mycobacterium tuberculosis virulence is highly metal-dependent with metal availability modulating the shift from the dormant to active states of M. tuberculosis infection. Rv0045c from M. tuberculosis is a proposed metabolic serine hydrolase whose folded stability is dependent on divalent metal concentration. Herein, we measured the divalent metal inhibition profile of the enzymatic activity of Rv0045c and found specific divalent transition metal cations) strongly inhibited its enzymatic activity. The metal cations bind allosterically, largely affecting values for k cat rather than K M . Removal of the artificial N-terminal 6xHis-tag did not change the metaldependent inhibition, indicating that the allosteric inhibition site is native to Rv0045c. To isolate the site of this allosteric regulation in Rv0045c, the structures of Rv0045c were determined at 1.8 Å and 2.0 Å resolution in the presence and absence of Zn 2+ with each structure containing a previously unresolved dynamic loop spanning the binding pocket. Through the combination of structural analysis with and without zinc and targeted mutagenesis, this metaldependent inhibition was traced to multiple chelating residues (H202A/ E204A) on a flexible loop, suggesting dynamic allosteric regulation of Rv0045c by divalent metals. Although serine hydrolases like Rv0045c are a large and diverse enzyme superfamily, this is the first structural confirmation of allosteric regulation of their enzymatic activity by divalent metals.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 80%

Section: Introductionmentioning

confidence: 98%

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Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C

et al. 2021

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“…Genus Salinisphaera inhabits brine water, such as marine and hypersaline environments, 37 and possessed esterase, which hydrolyzed the acyl group. 38 It is known that freshwater seminal plasma osmolarity is around 300 mOsmol kg −1 , which is equal to 1% NaCl concentration. 39 The results suggest that Salinisphaera sp.…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization of Microbiota Associated With Sperm of Malaysian Mahseer Tor tambroides

Koh

Nizam

Abduh

et al. 2019

Evol Bioinform Online

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Malaysian Mahseer ( Tor tambroides ) is considered as a good prospect for aquaculture in Malaysia. However, knowledge about Malaysian Mahseer-associated sperm microbiota is still limited, although some studies reported that sperm-related bacteria are a factor in the decline of sperm quality, as sperm may become the carrier of pathogenic bacteria to the egg. The goal of this study was to evaluate the sperm microbiota associated with Malaysian Mahseer from 3 different locations (Universiti Malaysia Terengganu [UMT], Ajil, and Pahang) using polymerase chain reaction denaturing gradient gel electrophoresis (PCR-DGGE) fingerprinting and to compare location differences by cluster analysis. Our results showed that the UMT sample had different sperm microbiota composition and a different trend in its relationship with sperm quality. Correlation analysis showed a relationship between bacterial diversity and sperm quality. Phylogenetic analysis indicated that sperm microbiota was composed of diverse phyla, including Proteobacteria, Firmicutes, and Actinobacteria. Interestingly, bacteria such as Salinisphaera sp., Pelomonas sp., and Staphylococcus spp. were detected in all the locations, suggesting that these bacteria are indigenous bacterial members of the Malaysian Mahseer sperm microbiota, although their function is still unclear.

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“…(Ryu et al, 2006), Salinisphaera sp. P7-4 (Kim et al, 2011), and Shewanella sp. Ke75 (Kim et al, 2013).…”

Section: Esterase Assaymentioning

confidence: 99%

Molecular Cloning, Purification, and Characterization of a Cold-Adapted Esterase from Photobacterium sp. MA1-3

Kim¹,

Heo²,

Nam³

et al. 2013

Fisheries and aquatic sciences

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The gene encoding an esterase from Photobacterium sp. MA1-3 was cloned in Escherichia coli using the shotgun method. The amino acid sequence deduced from the nucleotide sequence (948 bp) corresponded to a protein of 315 amino acid residues with a molecular weight of 35 kDa and a pI of 6.06. The deduced protein showed 74% and 68% amino acid sequence identities with the putative esterases from Photobacterium profundum SS9 and Photobacterium damselae, respectively. Absence of a signal peptide indicated that it was a cell-bound protein. Sequence analysis showed that the protein contained the signature G-X-S-X-G included in most serine-esterases and lipases. The MA1-3 esterase was produced in both soluble and insoluble forms when E. coli cells harboring the gene were cultured at 18°C. The enzyme was a serine-esterase and was active against C 2 , C 4 , C 8 and C 10 p-nitrophenyl esters. The optimum pH and temperature for enzyme activity were pH 8.0 and 30°C, respectively. Relative activity remained up to 45% even at 5°C with an activation energy of 7.69 kcal/mol, which indicated that it was a cold-adapted enzyme. Enzyme activity was inhibited by Cd 2+ , Cu 2+ , Zn 2+ , and Hg 2+ ions.

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A novel cold-adapted esterase from Salinisphaera sp. P7-4: Gene cloning, overproduction, and characterization

Cited by 10 publications

References 30 publications

Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C

Transition metal cation inhibition of Mycobacterium tuberculosis esterase RV0045C

Molecular Characterization of Microbiota Associated With Sperm of Malaysian Mahseer Tor tambroides

Molecular Cloning, Purification, and Characterization of a Cold-Adapted Esterase from Photobacterium sp. MA1-3

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