Escherichia coli Leader Peptidase: Production of an Active Form Lacking a Requirement for Detergent and Development of Peptide Substrates

Kuo, David; Chan, Hedy; Wilson, Carol J.; Griffin, Patrick R.; Williams, Hollis R.; Knight, Wilson B.

doi:10.1006/abbi.1993.1283

Cited by 61 publications

(53 citation statements)

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“…The E. eoli leader peptidase is not inhibited by standard [13,14]. Leader peptidases are mechanistically novel serine proteases that utilize a serine/lysine catalytic dyad similar to that found in 13-1actamase [15].…”

Section: Introductionmentioning

confidence: 91%

Inhibition by penem of processing peptidases from cyanobacteria and chloroplast thylakoids

1996

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Proteins targeted to the thylakoid lumen of plants and cyanobaeteria and the periplasmic space of cyanobacteria are synthesised with N-terminal presequences which are removed following translocation across the membrane. These presequences are thought to direct translocation of the preprotein by a sec-type pathway. Detergent extracts of cyanobacterial and chloroplast membranes contain enzymes which are capable of processing precursors to the mature size. We show that the processing of a range of precursors by both cyanobacterial and chloroplast enzymes is inhibited by the penem SB216357. This is the first report of an inhibitor of these enzymes and indicates that they are type 1 signal peptidases.

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Section: Introductionmentioning

confidence: 91%

Inhibition by penem of processing peptidases from cyanobacteria and chloroplast thylakoids

1996

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“…First, these proteases failed to be inhibited by inhibitors against the aspartic acid, metallo, serine, and cysteine protease groups (Zwizinski et al 1981;Black et al 1992;Kuo et al 1993). Second, the Escherichia coli signal peptidase had a critical serine (Ser90) and lysine (Lys145) residue (Sung and Dalbey 1992;Black 1993;Tschantz et al 1993) but no critical histidine residue (Sung and Dalbey 1992), and both residues are absolutely conserved in evolution within the bacterial, chloroplast, and mitochondrial signal peptidase family members (Paetzel et al 2002b).…”

Section: Type I Signal Peptidasesmentioning

confidence: 99%

Unconventional serine proteases: Variations on the catalytic Ser/His/Asp triad configuration

2008

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Serine proteases comprise nearly one-third of all known proteases identified to date and play crucial roles in a wide variety of cellular as well as extracellular functions, including the process of blood clotting, protein digestion, cell signaling, inflammation, and protein processing. Their hallmark is that they contain the so-called ''classical'' catalytic Ser/His/Asp triad. Although the classical serine proteases are the most widespread in nature, there exist a variety of ''nonclassical'' serine proteases where variations to the catalytic triad are observed. Such variations include the triads Ser/His/Glu, Ser/ His/His, and Ser/Glu/Asp, and include the dyads Ser/Lys and Ser/His. Other variations are seen with certain serine and threonine peptidases of the Ntn hydrolase superfamily that carry out catalysis with a single active site residue. This work discusses the structure and function of these novel serine proteases and threonine proteases and how their catalytic machinery differs from the prototypic serine protease class.

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“…In addition to naturally occurring precursor protein substrates, E. coli signal peptidase can process short, synthetic peptide substrates based on the cleavage site region of pre-maltose binding protein (Dev et al, 1990) and M13 procoat (Dierstein & Wickner, 1986;Kuo et al, 1993). However, the peptides are poor substrates for signal peptidase with a k,, of 119 h" and a K,,, of 1 mM for the best substrate (Dev et al, 1990).…”

Section: Substrates and Inhibitorsmentioning

confidence: 99%

The chemistry and enzymology of the type I signal peptidases

et al. 1997

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The discovery that proteins exported from the cytoplasm are typically synthesized as larger precursors with cleavable signal peptides has focused interest on the peptidases that remove the signal peptides. Here, we review the membranebound peptidases dedicated to the processing of protein precursors that are found in the plasma membrane of prokaryotes and the endoplasmic reticulum, the mitochondrial inner membrane, and the chloroplast thylakoidal membrane of eukaryotes. These peptidases are termed type I signal (or leader) peptidases. They share the unusual feature of being resistant to the general inhibitors of the four well-characterized peptidase classes. The eukaryotic and prokaryotic signal peptidases appear to belong to a single peptidase family. This review emphasizes the evolutionary concepts, current knowledge of the catalytic mechanism, and substrate specificity requirements of the signal peptidases.

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Escherichia coli Leader Peptidase: Production of an Active Form Lacking a Requirement for Detergent and Development of Peptide Substrates

Cited by 61 publications

References 0 publications

Inhibition by penem of processing peptidases from cyanobacteria and chloroplast thylakoids

Inhibition by penem of processing peptidases from cyanobacteria and chloroplast thylakoids

Unconventional serine proteases: Variations on the catalytic Ser/His/Asp triad configuration

The chemistry and enzymology of the type I signal peptidases

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