Purification and partial characterization of the 7-d-glutamyl-l-di-amino acid endopeptidase ii from bacillus sphaericus

Bourgogne, Thierry; Vacheron, Marie‐Jeanne; Guinand, Micheline; Michel, Georges

doi:10.1016/0020-711x(92)90041-x

Cited by 16 publications

(14 citation statements)

References 13 publications

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“…Another Bacillus subtilis enzyme, YwtD, specifically cleaves the γ-glutamyl bond between D-glutamic acid and L-glutamic acid of γ-polyglutamic acid (Suzuki and Tahara, 2003). DPP VI is involved in cell sporulation and hydrolyzes γ-D-Glu-DAP(Lys) linkages in peptides that have a free N-terminal L-alanine (Bourgogne et al, 1992). Many members of the CHAP family are MurNAc amidases that cleave the N-acetylmuramyl-L-alanine bond, but other linkage preferences are also observed.…”

Section: Introductionmentioning

confidence: 99%

Structural Basis of Murein Peptide Specificity of a γ-D-Glutamyl-L-Diamino Acid Endopeptidase

Sudek

McMullan

et al. 2009

Structure

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Crystal structures of two homologous peptidases from cyanobacteria Anabaena variabilis and Nostoc punctiforme at 1.05 Å and 1.60 Å resolution represent the first structures of a large class of cell-wall, cysteine peptidases that contain an N-terminal bacterial SH3-like domain (SH3b) and a C-terminal NlpC/P60 cysteine peptidase domain. The NlpC/P60 domain is a primitive, papain-like peptidase in the CA clan of cysteine peptidases with a Cys126/His176/His188 catalytic triad and a conserved catalytic core. We deduced from structure and sequence analysis, and then experimentally, that that these two proteins act as γ-D-glutamyl-L-diamino acid endopeptidases (EC 3.4.22.-). The active site is located near the interface between the SH3b and NlpC/P60 domains, where the SH3b domain may help define substrate specificity, instead of functioning as a targeting domain, so that only muropeptides with an N-terminal L-alanine can bind to the active site.

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Section: Introductionmentioning

confidence: 99%

Structural Basis of Murein Peptide Specificity of a γ-D-Glutamyl-L-Diamino Acid Endopeptidase

Sudek

McMullan

et al. 2009

Structure

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“…Identities are shown by vertical bars.mined experimentally on the purified protein[4] and the calculated relative molecular mass 30 604 compared well with the 28-kDa value derived from SDS gel electrophoresis[4]. Identities are shown by vertical bars.mined experimentally on the purified protein[4] and the calculated relative molecular mass 30 604 compared well with the 28-kDa value derived from SDS gel electrophoresis[4].…”

mentioning

confidence: 71%

“…The B. sphaericus endopeptidase I1 is sensitive to thiol-group reagents, suggesting that it might be a eysteine peptidase [4]. The occurrence of an odd number of cysteines at positions 55, 178 and 182, respectively, is compatible with such a mechanism.…”

Section: Discussionmentioning

confidence: 99%

“…has bccn purified to protein homogeneity and its 38-amino acid N-terminal region has been sequenced [4]. Among the hydrolases that appear to be related to sporulation in Bacillus sphaericus, the y-D-glutamyl-t.-diamino acid endopeptidase I!…”

Section: Introductionmentioning

confidence: 99%

“…The MI-L38 amino acid sequence is that determined by chemical sequencing of the purified endopeptidase II[4],[4]. I. DNA probe constructkm.…”

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confidence: 99%

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Cloning and nucleotide sequence of the gene encoding the γ-?-glutamyl-?-diamino acid endopeptidase II of Bacillus sphaericus

Hourdou¹

1992

FEMS Microbiology Letters

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The gene encoding the Bacillus sphaericus gamma-D-glutamyl-L-diamino acid endopeptidase II, a cytoplasmic enzyme involved in cell sporulation [1], contains the information for a 271-amino acid protein devoid of a signal peptide. The endopeptidase lacks sequence relatedness with other proteins of known primary structure except that its C-terminal region has significant similarity with the C-terminal region of the 54-kDa P54 protein of Enterococcus faecium, of unknown function [2].

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Dermatophagoides pteronyssinus lytFM encoding an NlpC/P60 endopeptidase is also present in mite‐associated bacteria that express LytFM variants

2017

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The bodies and faecal pellets of the house dust mite ( HDM ), Dermatophagoides pteronyssinus , are the source of many allergenic and nonallergenic proteins. One of these, the 14‐ kD a bacteriolytic enzyme Lyt FM , originally isolated from the spent HDM growth medium, may contribute to bacteriolytic activity previously detected by zymography at 14 kD a in the culture supernatants of some bacterial species isolated from surface‐sterilised HDM . Based on previously reported findings of lateral gene transfer between microbes and their eukaryotic hosts, we investigated the presence of lyt FM in the genomes of nine Gram‐positive bacteria from surface‐sterilised HDM , and the expression by these isolates of Lyt FM and its variants Lyt FM 1/Lyt FM 2. The lyt FM gene was detected by PCR in the genomes of three of the isolates: Bacillus licheniformis strain 1, B. licheniformis strain 2 and Staphylococcus aureus . Expression of the variant Lyt FM 1 was detected in culture supernatants of these bacteria by mass spectrometry ( MS ) and ELISA , and the bacterial Lyt FM proteins were shown by zymography to be able to hydrolyse peptidoglycan. Our previous reports of Lyt FM homologues in other mite species and their phylogenetic analysis had suggested that they originated from a common mite ancestor. The phylogenetic analysis reported herein and the detection of other D. pteronyssinus proteins by MS in the culture supernatants of the three isolates that secreted Lyt FM 1 further support the hypothesis of lateral gene transfer to the bacterial endosymbionts from their HDM host. The complete sequence homology observed between the genes amplified from the microbes and those in their eukaryotic host indicated that the lateral gene transfer was an event that occurred recently.

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Purification and partial characterization of the 7-d-glutamyl-l-di-amino acid endopeptidase ii from bacillus sphaericus

Cited by 16 publications

References 13 publications

Structural Basis of Murein Peptide Specificity of a γ-D-Glutamyl-L-Diamino Acid Endopeptidase

Structural Basis of Murein Peptide Specificity of a γ-D-Glutamyl-L-Diamino Acid Endopeptidase

Cloning and nucleotide sequence of the gene encoding the γ-?-glutamyl-?-diamino acid endopeptidase II of Bacillus sphaericus

Dermatophagoides pteronyssinus lytFM encoding an NlpC/P60 endopeptidase is also present in mite‐associated bacteria that express LytFM variants

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