Cao_2017_Sci.Rep_7_2141

Reference

Title : Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context - Cao_2017_Sci.Rep_7_2141
Author(s) : Cao X , Zhu L , Hu Z , Cronan JE
Ref : Sci Rep , 7 :2141 , 2017
Abstract : BioH is an alpha/beta-hydrolase required for synthesis of the pimelate moiety of biotin in diverse bacteria. The bioH gene is found in different genomic contexts. In some cases (e.g., Escherichia coli) the gene is not located within a biotin synthetic operon and its transcription is not coregulated with the other biotin synthesis genes. In other genomes such as Pseudomonas aeruginosa the bioH gene is within a biotin synthesis operon and its transcription is coregulated with the other biotin operon genes. The esterases of pimelate moiety synthesis show remarkable genomic plasticity in that in some biotin operons bioH is replaced by other alpha/ss hydrolases of diverse sequence. The "wild card" nature of these enzymes led us to compare the paradigm "freestanding" E. coli BioH with the operon-encoded P. aeruginosa BioH. We hypothesized that the operon-encoded BioH might differ in its expression level and/or activity from the freestanding BioH gene. We report this is not the case. The two BioH proteins show remarkably similar hydrolase activities and substrate specificity. Moreover, Pseudomonas aeruginosa BioH is more highly expressed than E. coli BioH. Despite the enzymatic similarities of the two BioH proteins, bioinformatics analysis places the freestanding and operon-encoded BioH proteins into distinct clades.
ESTHER : Cao_2017_Sci.Rep_7_2141
PubMedSearch : Cao_2017_Sci.Rep_7_2141
PubMedID: 28526858
Gene_locus related to this paper: fratt-q5nga8 , pseae-PA0502

Related information

Gene_locus related to this paper: fratt-q5nga8 , pseae-PA0502

Citations formats

Cao X, Zhu L, Hu Z, Cronan JE (2017)
Expression and Activity of the BioH Esterase of Biotin Synthesis is Independent of Genome Context
Sci Rep 7 :2141

Cao X, Zhu L, Hu Z, Cronan JE (2017)
Sci Rep 7 :2141