Characterization of a new heterotrophic nitrification bacterium Pseudomonas sp. strain JQ170 and functional identification of nap gene in nitrite production

Functional characterization of unknown genes is currently a major task in biology. The search for gene function involves a combination of various in silico, in vitro and in vivo approaches. Available knowledge from the study of more than 21 LysR-type regulators in Escherichia coli has facilitated the classification of new members of the family. From sequence similarities and its location on the E. coli chromosome, it is suggested that ygiP encodes a lysR regulator controlling the expression of a neighbouring operon; this operon encodes the two subunits of tartrate dehydratase (TtdA, TtdB) and YgiE, an integral inner-membrane protein possibly involved in tartrate uptake. Expression of tartrate dehydratase, which converts tartrate to oxaloacetate, is required for anaerobic growth on glycerol as carbon source in the presence of tartrate. Here, it has been demonstrated that disruption of ygiP, ttdA or ygjE abolishes tartrate-dependent anaerobic growth on glycerol. It has also been shown that tartrate-dependent induction of the ttdA-ttdB-ygjE operon requires a functional YgiP.

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Isolation and characterization of a novel rhamnolipid producer Pseudomonas sp. LGMS7 from a highly contaminated site in Ain El Arbaa region of Ain Temouchent, Algeria

3 Biotech ◽

10.1007/s13205-021-02751-6 ◽

2021 ◽

Vol 11 (4) ◽

Author(s):

Abdelkrim Chaida ◽

Alif Chebbi ◽

Farid Bensalah ◽

Andrea Franzetti

Keyword(s):

Contaminated Site ◽

Pseudomonas Sp ◽

Isolation And Characterization

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Mucopolysaccharidases from Pseudomonas sp.. Isolation and partial characterization of constitutive enzymes involved in the degradation of keratan sulfate and chondroitin sulfate

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1986.tb10134.x ◽

1986 ◽

Vol 161 (1) ◽

pp. 139-147 ◽

Cited By ~ 6

Author(s):

Denise S. P. Q. HORTON ◽

Yara M. MICHELACCI

Keyword(s):

Chondroitin Sulfate ◽

Keratan Sulfate ◽

Partial Characterization ◽

Pseudomonas Sp

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Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas sp. S9

Bioscience Reports ◽

10.1042/bsr20170001 ◽

2017 ◽

Vol 37 (3) ◽

Author(s):

Lifang Sun ◽

Pu Chen ◽

Yintao Su ◽

Zhixiong Cai ◽

Lingwei Ruan ◽

...

Keyword(s):

Crystal Structure ◽

Sodium Dodecyl ◽

Titration Calorimetry ◽

Pseudomonas Sp ◽

Sterol Carrier Protein ◽

Dimerization Domain ◽

Alkyl Chains ◽

Hydrolysis Of

A novel alkylsulfatase from bacterium Pseudomonas sp. S9 (SdsAP) was identified as a thermostable alkylsulfatases (type III), which could hydrolyze the primary alkyl sulfate such as sodium dodecyl sulfate (SDS). Thus, it has a potential application of SDS biodegradation. The crystal structure of SdsAP has been solved to a resolution of 1.76 Å and reveals that SdsAP contains the characteristic metallo-β-lactamase-like fold domain, dimerization domain, and C-terminal sterol carrier protein type 2 (SCP-2)-like fold domain. Kinetic characterization of SdsAP to SDS by isothermal titration calorimetry (ITC) and enzymatic activity assays of constructed mutants demonstrate that Y246 and G263 are important residues for its preference for the hydrolysis of ‘primary alkyl’ chains, confirming that SdsAP is a primary alkylsulfatase.

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