Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase

R. Suresh Kumar; James A. Brannigan; Asmita A. Prabhune; Archana V. Pundle; Guy G. Dodson; Eleanor J. Dodson; C. G. Suresh

doi:10.1074/jbc.M604172200

Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase

R. Suresh Kumar, James A. Brannigan, Asmita A. Prabhune, Archana V. Pundle, Guy G. Dodson, Eleanor J. Dodson, C. G. Suresh

Chemistry

Research output: Contribution to journal › Article › peer-review

Abstract

Bile salt hydrolase (BSH) is an enzyme produced by the intestinal microflora that catalyzes the deconjugation of glycine- or taurine-linked bile salts. The crystal structure of BSH reported here from Bifidobacterium longum reveals that it is a member of N-terminal nucleophil hydrolase structural superfamily possessing the characteristic alpha beta beta alpha tetra-lamellar tertiary structure arrangement. Site-directed mutagenesis of the catalytic nucleophil residue, however, shows that it has no role in zymogen processing into its corresponding active form. Substrate specificity was studied using Michaelis-Menten and inhibition kinetics and fluorescence spectroscopy. These data were compared with the specificity profile of BSH from Clostridium perfrigens and pencillin V acylase from Bacillus sphaericus, for both of which the three-dimensional structures are available. Comparative analysis shows a gradation in activity toward common substrates, throwing light on a possible common route toward the evolution of pencillin V acylase and BSH.

Original language	English
Pages (from-to)	32516-32525
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	281
Issue number	43
DOIs	https://doi.org/10.1074/jbc.M604172200
Publication status	Published - 27 Oct 2006

Keywords

LACTIC-ACID BACTERIA
QUANTITATIVE-DETERMINATION
LACTOBACILLUS-PLANTARUM
CHOLESTEROL
DECONJUGATION
PURIFICATION
CLONING
EXPRESSION
GENE

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10.1074/jbc.M604172200

Cite this

Kumar, R. S., Brannigan, J. A., Prabhune, A. A., Pundle, A. V., Dodson, G. G., Dodson, E. J., & Suresh, C. G. (2006). Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase. Journal of Biological Chemistry, 281(43), 32516-32525. https://doi.org/10.1074/jbc.M604172200

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title = "Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase",

abstract = "Bile salt hydrolase (BSH) is an enzyme produced by the intestinal microflora that catalyzes the deconjugation of glycine- or taurine-linked bile salts. The crystal structure of BSH reported here from Bifidobacterium longum reveals that it is a member of N-terminal nucleophil hydrolase structural superfamily possessing the characteristic alpha beta beta alpha tetra-lamellar tertiary structure arrangement. Site-directed mutagenesis of the catalytic nucleophil residue, however, shows that it has no role in zymogen processing into its corresponding active form. Substrate specificity was studied using Michaelis-Menten and inhibition kinetics and fluorescence spectroscopy. These data were compared with the specificity profile of BSH from Clostridium perfrigens and pencillin V acylase from Bacillus sphaericus, for both of which the three-dimensional structures are available. Comparative analysis shows a gradation in activity toward common substrates, throwing light on a possible common route toward the evolution of pencillin V acylase and BSH.",

keywords = "LACTIC-ACID BACTERIA, QUANTITATIVE-DETERMINATION, LACTOBACILLUS-PLANTARUM, CHOLESTEROL, DECONJUGATION, PURIFICATION, CLONING, EXPRESSION, GENE",

author = "Kumar, {R. Suresh} and Brannigan, {James A.} and Prabhune, {Asmita A.} and Pundle, {Archana V.} and Dodson, {Guy G.} and Dodson, {Eleanor J.} and Suresh, {C. G.}",

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doi = "10.1074/jbc.M604172200",

language = "English",

volume = "281",

pages = "32516--32525",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

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Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase. / Kumar, R. Suresh; Brannigan, James A.; Prabhune, Asmita A. et al.
In: Journal of Biological Chemistry, Vol. 281, No. 43, 27.10.2006, p. 32516-32525.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase

AU - Kumar, R. Suresh

AU - Brannigan, James A.

AU - Prabhune, Asmita A.

AU - Pundle, Archana V.

AU - Dodson, Guy G.

AU - Dodson, Eleanor J.

AU - Suresh, C. G.

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Y1 - 2006/10/27

N2 - Bile salt hydrolase (BSH) is an enzyme produced by the intestinal microflora that catalyzes the deconjugation of glycine- or taurine-linked bile salts. The crystal structure of BSH reported here from Bifidobacterium longum reveals that it is a member of N-terminal nucleophil hydrolase structural superfamily possessing the characteristic alpha beta beta alpha tetra-lamellar tertiary structure arrangement. Site-directed mutagenesis of the catalytic nucleophil residue, however, shows that it has no role in zymogen processing into its corresponding active form. Substrate specificity was studied using Michaelis-Menten and inhibition kinetics and fluorescence spectroscopy. These data were compared with the specificity profile of BSH from Clostridium perfrigens and pencillin V acylase from Bacillus sphaericus, for both of which the three-dimensional structures are available. Comparative analysis shows a gradation in activity toward common substrates, throwing light on a possible common route toward the evolution of pencillin V acylase and BSH.

AB - Bile salt hydrolase (BSH) is an enzyme produced by the intestinal microflora that catalyzes the deconjugation of glycine- or taurine-linked bile salts. The crystal structure of BSH reported here from Bifidobacterium longum reveals that it is a member of N-terminal nucleophil hydrolase structural superfamily possessing the characteristic alpha beta beta alpha tetra-lamellar tertiary structure arrangement. Site-directed mutagenesis of the catalytic nucleophil residue, however, shows that it has no role in zymogen processing into its corresponding active form. Substrate specificity was studied using Michaelis-Menten and inhibition kinetics and fluorescence spectroscopy. These data were compared with the specificity profile of BSH from Clostridium perfrigens and pencillin V acylase from Bacillus sphaericus, for both of which the three-dimensional structures are available. Comparative analysis shows a gradation in activity toward common substrates, throwing light on a possible common route toward the evolution of pencillin V acylase and BSH.

KW - LACTIC-ACID BACTERIA

KW - QUANTITATIVE-DETERMINATION

KW - LACTOBACILLUS-PLANTARUM

KW - CHOLESTEROL

KW - DECONJUGATION

KW - PURIFICATION

KW - CLONING

KW - EXPRESSION

KW - GENE

U2 - 10.1074/jbc.M604172200

DO - 10.1074/jbc.M604172200

M3 - Article

SN - 0021-9258

VL - 281

SP - 32516

EP - 32525

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 43

ER -