Comparison of the sequences of class A beta-lactamases and of the secondary structure elements of penicillin-recognizing proteins

Joris, Bernard; Ledent, Philippe; Dideberg, Otto; Fonzé, E.; Lamotte‐Brasseur, Josette; Kelly, Judith A.; Ghuysen, Jean‐Marie; Frère, Jean‐Marie

doi:10.1128/aac.35.11.2294

Cited by 155 publications

(139 citation statements)

References 52 publications

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“…The major secondary structural elements of t;Dpeptidases and serine fl-lactamases can be superposed on each other. An important structural difference, which may somehow influence substrate recognition, is the inverted orientation of helix ~10 in the class C fllaetarnase [5]. These relationships support the concept that the AmpC protein may recognize both p-lactams and LD-peptides as substrates.…”

Section: Growth Rate Control Of Ampc Syn-thesis and Murein Structurementioning

confidence: 54%

“…In the presence of penicillin, the Dp-peptidases form a stable penicilloyl enzyme, whereas the serinefl-lactamases ferm a penicilloyl enzyme which is hydrolytically labile. Since Dt)-peptidases and serine ~-lactamases of class A and C exhibit similar tertiary structures, it is now believed that they evolved divergently from an ancestral enzyme [5]. However, the serine fl-lactamases of class A are distinct from the class C enzymes (AmpC) [5].…”

Section: Meso-diaminopimelyl-d-alanyl-d-alanine (L-ala-d-?-glu-(l)-m-mentioning

confidence: 99%

“…Since Dt)-peptidases and serine ~-lactamases of class A and C exhibit similar tertiary structures, it is now believed that they evolved divergently from an ancestral enzyme [5]. However, the serine fl-lactamases of class A are distinct from the class C enzymes (AmpC) [5]. Some relationships between peptidoglycan structure and the regulation of enterobacterial AmpC ~ynthesis are difficult to interpret in terms of the DD-peptidase analogy.…”

Section: Meso-diaminopimelyl-d-alanyl-d-alanine (L-ala-d-?-glu-(l)-m-mentioning

confidence: 99%

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Coordinate regulation of murein peptidase activity and AmpC β‐lactamase synthesis in Escherichia coli

Bishop¹,

Weiner²

1992

FEBS Letters

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In the periplasmic space of F.sche~'ichia coil, the (L)-m-A,pm-(D)-m-A,pm pcptid¢, the lipoprotein, and the AmpC fl-lactamas¢ are controlled by growth rate. To explain this coordinate regulation, it is proposed that the AmpC protein functions as an LD-endopeptidase in addition to its known function as a fl-lactamas¢. As LD-peptides, vo-peptides and fl-lactams are structurally similar, to-peptidases may belong to the larger family of DD-peptidases and serine ~-lactamases. In contrast to K coll. many related bacteria possess an inducible AmpC protein. Several gene systems necessary for AmpC induction are known to affect various aspects of peptidoglyean metabolism, It is proposed that AmpC induction ¢o=urs indirectly via a recyclabl¢ e¢ll wall pcptid¢.

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Section: Growth Rate Control Of Ampc Syn-thesis and Murein Structurementioning

confidence: 54%

Section: Meso-diaminopimelyl-d-alanyl-d-alanine (L-ala-d-?-glu-(l)-m-mentioning

confidence: 99%

Section: Meso-diaminopimelyl-d-alanyl-d-alanine (L-ala-d-?-glu-(l)-m-mentioning

confidence: 99%

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Coordinate regulation of murein peptidase activity and AmpC β‐lactamase synthesis in Escherichia coli

Bishop¹,

Weiner²

1992

FEBS Letters

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“…1). FimD is predicted to be a smaller and more distant relative of PBP1 A, but its sequence nevertheless has all the criticarresidues COI1-served in the PBP family (Joris et al, 1991). The transcriptional coupling of fimD to fimbrial genes implies that it plays some part in fimbrial biology (Hobbs et al, 1991).…”

Section: Other Connectionsmentioning

confidence: 99%

Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein‐secretion apparatus: a general system for the formation of surface‐associated protein complexes

Hobbs

Mattick

1993

Molecular Microbiology

361

286

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Summary The Pseudomonas aeruginosa genes pilB‐D and pilQ are necessary for the assembly of type 4 fimbriae. Homologues of these genes and of the subunit (pilin) gene have been described in various different bacterial species, but not always in association with type 4 fimbrial biosynthesis and function. Pil‐like proteins are also involved in protein secretion, DNA transfer by conjugation and transformation, and morphogenesis of filamentous bacteriophages. It seems likely that the Pil homologues function in the processing and export of proteins resembling type 4 fimbrial sub‐units, and in their organization into fimbrial‐like structures. These may either be true type 4 fimbriae, or components of protein complexes which act in the transport of macromolecules (DNA or protein) into or out of the cell. Some PilB‐like and PilQ‐like proteins are apparently also involved in the assembly of non‐type 4 polymeric structures (filamentous phage virions and conjugative pili). The diverse studies summarized in this review are providing insight into an extensive infrastructural system which appears to be utilized in the formation of a variety of cell surface‐associated complexes.

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“…It has been characterized and named D-aminopeptidase (Dap) (E.C 3.4.11.19) [10,11]. Its sequence exhibits 25% identity with that of the Streptomyces R61 DD-carboxypeptidase and the residues most important for the catalytic mechanism of i-lactamases and DD-carboxypeptidases [11][12][13][14][15] appeared to be conserved. Here we report the isolation and purification of a similar D-aminopeptidase from O. anthropi LMG7991.…”

mentioning

confidence: 99%

Two new aminopeptidases from Ochrobactrum anthropi active on D-alanyl-p-nitroanilide

Fanuel

Thamm

Kostanjevečki³

et al. 1999

CMLS, Cell. Mol. Life Sci.

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Abstract.Two new enzymes which hydrolyse D-alanyl-on the tripeptide L-Ala-Gly-Gly but it was not possible p-nitroanilide have been detected in Ochrobactrum an-to be certain that the same protein was responsible for thropi LMG7991 extracts. The first enzyme, DmpB, was both p-nitroanilide and peptide hydrolysing activities. purified to homogeneity and found to be homologous to The gene encoding the DmpA protein was cloned and sequenced. The deduced protein sequence exhibits varythe Dap protein produced by O. anthropi SCRC C1-38 (ATCC49237). The second enzyme, DmpA, exhibits a ing degrees of similarity with those corresponding to similar substrate profile when tested on p-nitroanilide several open reading frames found in the genomes of other prokaryotic organisms, including Mycobacteria. derivatives of glycine and L/D-alanine, but the amounts produced by the Ochrobactrum strain were not sufficient None of these gene products has been isolated or characterised, but a tentative relationship can be proposed with to allow complete purification. Interestingly, the DmpA preparation also exhibited an L-aminopeptidase activity the NylC amidase from Fla6obacterium sp. K172.Key words. Peptidase; stereospecificity; amidohydrolase.Aminopeptidases release the amino-terminal residue from peptide substrates. Most are L-aminopeptidases and exhibit a wide variety of molecular masses, quaternary structures, catalytic residues and specificity profiles [1 -10]. So far, the only aminopeptidase active on peptides containing N-terminal D-residues is that from Ochrobactrum anthropi SCRC C1-38. It has been characterized and named D-aminopeptidase (Dap) (E.C 3.4.11.19) [10,11]. Its sequence exhibits 25% identity with that of the Streptomyces R61 DD-carboxypeptidase and the residues most important for the catalytic mechanism of i-lactamases and DD-carboxypeptidases [11][12][13][14][15] appeared to be conserved. Here we report the isolation and purification of a similar D-aminopeptidase from O. anthropi LMG7991. Moreover, the same strain produces a second enzyme which hydrolyses D-alanyl-pnitroanilide but not its N-acetylated derivative, and thus represents a new potential member of the Daminopeptidase family. The study of D-aminopeptidases will contribute general information on this poorly characterized enzyme group and will help to elucidate the possible evolutionary relationship between D-aminopep-* Corresponding author.

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Comparison of the sequences of class A beta-lactamases and of the secondary structure elements of penicillin-recognizing proteins

Cited by 155 publications

References 52 publications

Coordinate regulation of murein peptidase activity and AmpC β‐lactamase synthesis in Escherichia coli

Coordinate regulation of murein peptidase activity and AmpC β‐lactamase synthesis in Escherichia coli

Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein‐secretion apparatus: a general system for the formation of surface‐associated protein complexes

Two new aminopeptidases from Ochrobactrum anthropi active on D-alanyl-p-nitroanilide

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