Amino Acid Sequences of Metalloendopeptidases Specific for Acyl-Lysine Bonds from Grifola frondosa and Pleurotus ostreatus Fruiting Bodies

Nonaka, Takashi; Dohmae, Naoshi; Hashimoto, Yohichi; Takio, Koji

doi:10.1074/jbc.272.48.30032

Cited by 56 publications

(34 citation statements)

References 35 publications

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“…2B). When mature enzymes were aligned, it was a puzzle why GfMEP is shorter by one residue at the amino terminus among aspzincins of known amino termini (Nonaka et al, 1997). The sequence at the carboxyl terminus of the prodomain may provide the answer.…”

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confidence: 99%

“…Oligonucleotide sequences and directions of the primers used for 5Ј-and 3Ј-RACEs are indicated by horizontal arrows. Residues essential for the enzyme activity of aspzincins are underlined (Hori et al, 2001;Nonaka et al, 1997) and N-terminal Thr of mature GfMEP is circled. Signal peptidase cleavage site is indicated by a vertical arrow.…”

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confidence: 99%

“…Alignment was obtained with the program Clustal W multiple sequence alignment (Thompson et al, 1994). Because mature aspzincin enzymes were already aligned and discussed (Hori et al, 2001;Nonaka et al, 1997), alignment of preprosequences is shown in the figure. In the case of AhMEP, although the amino terminus of the Signal peptidase cleavage sites were estimated by SignalP V1.1 except for experimentally proven GfMEP (this paper) and penicillolysin (Matsumoto et al, 1994).…”

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PCR cloning and heterologous expression of cDNA encoding a peptidyl-Lys metalloendopeptidase precursor of Grifola frondosa.

Saito

Dohmae

Tsujimoto

et al. 2002

J. Gen. Appl. Microbiol.

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Metalloendopeptidases (MEPs) are widely distributed from bacteria to mammals, and they carry out various important roles. Many MEPs have been classified into two major families, "gluzincins" and "metzincins," according to the structural topology around the active site (Bode et al., 1993;Hooper, 1994;Rawlings and Barrett, 1995). We have purified and characterized uniquely specific peptidyl-Lys MEPs from edible mushrooms, Grifola frondosa (GfMEP) (Nonaka et al

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PCR cloning and heterologous expression of cDNA encoding a peptidyl-Lys metalloendopeptidase precursor of Grifola frondosa.

Saito

Dohmae

Tsujimoto

et al. 2002

J. Gen. Appl. Microbiol.

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“…The predicted amino acid sequence, including aspartic acid and glutamic acid, of deuterolysin (17) has strong similarity to other members of the deuterolysin family: MEP20 from Aspergillus flavus (25) and Aspergillus fumigatus (26), metalloendopeptidases from Grifola frondosa and Pleurotus ostreatus (27), and penicillolysin (23). This finding may indicate that enzymes in the deuterolysin family are coded for by evolutionarily related genes at the enzymatic level.…”

Section: Zn Binding Assay Based On Site-directed Mutagenesis Experimmentioning

confidence: 70%

Aspzincin, a Family of Metalloendopeptidases with a New Zinc-binding Motif

Fushimi¹,

Ee²,

Nakajima³

et al. 1999

Journal of Biological Chemistry

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“…We recently reported a Lys-N-based technique, which is advantageous over tryptic digestion because it incorporates only a single 18 O atom into the carboxyl terminus of each proteolytically generated peptide (5). Lys-N is a metalloendopeptidase (peptidyl-Lys metalloendopeptidase, EC 3.4.24.20) that cleaves specifically peptidyl-lysine bonds (-XLys-) in proteins and peptides (6). In this initial study with several model proteins the unique single 18 O atom incorporation property of Lys-N was shown to provide accurate quan-tification results.…”

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Peptidyl-Lys Metalloendopeptidase-catalyzed 18O Labeling for Comparative Proteomics

Rao¹,

Palamalai²,

Dunlevy

et al. 2005

Molecular & Cellular Proteomics

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We recently proposed a comparative proteomic method utilizing proteolytic 18 Large scale quantitative measurements of protein expressions in different sets of samples (comparative proteomics) are expected to be critical to the advance of our understanding of physiological processes and disease mechanisms. Although 2D 1 PAGE-based methods have been the primary choice in comparative proteomics, 2D gels are cumbersome to run, have a poor dynamic range, and are biased toward abundant and soluble proteins (1). Therefore alternative methods have been actively sought. One such method is mass spectrometry-based in vitro stable isotope labeling in which proteins from the control and experimental samples are proteolytically digested. The generated peptides from the control sample are then labeled with naturally abundant (light) isotope(s), whereas the peptides from the experimental sample are labeled with its heavier isotope(s) or vice versa. The samples are then mixed together in equal proportions, and the relative abundance of each particular peptide from the two samples is determined by mass spectrometry. By comparing the peak areas or intensities of the light and heavy peptides, the relative abundance of each particular peptide can be determined; this equals the relative abundance in the original samples of the parent protein from which the peptide was generated.Among the mass spectrometry-based in vitro stable isotope labeling methods, the proteolytic 18 O labeling method (2) is particularly attractive because it has the least technical variations. In this method, the stable isotopic ( 18 O atom) labeling of peptides is achieved concurrently with the proteolytic digestion of proteins. Therefore the yield of each isotopically labeled peptide depends only on the effectiveness of proteolytic digestion in both samples compared. In contrast, the other in vitro stable isotope labeling methods (such as the isotope-coded affinity tag method (3)) have the isotopic labeling and proteolytic digestion of proteins occurring at different steps, meaning that the yield of each isotopically labeled peptide has greater variability because it depends on both the yield of the isotope labeling and the effectiveness of the proteolytic digestion.Trypsin has been the protease most utilized in proteolytic 18 O labeling methods. However, it is known that trypsin generates a mixture of isotopic isoforms resulting from the variable incorporation of either one or two 18 O atoms ( 18 O 1 / 18 O 2 ) into each peptide (4). This not only makes quantification of the peptides complicated but also increases the error in the experimentally determined 16 O-and 18 O-labeled peptides ratios. We recently reported a Lys-N-based technique, which is advantageous over tryptic digestion because it incorporates only a single 18 O atom into the carboxyl terminus of each proteolytically generated peptide (5). Lys-N is a metalloendopeptidase (peptidyl-Lys metalloendopeptidase, EC 3.4.24.20) that cleaves specifically peptidyl-lysine bonds (-XLys-) in proteins and pe...

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Amino Acid Sequences of Metalloendopeptidases Specific for Acyl-Lysine Bonds from Grifola frondosa and Pleurotus ostreatus Fruiting Bodies

Cited by 56 publications

References 35 publications

PCR cloning and heterologous expression of cDNA encoding a peptidyl-Lys metalloendopeptidase precursor of Grifola frondosa.

PCR cloning and heterologous expression of cDNA encoding a peptidyl-Lys metalloendopeptidase precursor of Grifola frondosa.

Aspzincin, a Family of Metalloendopeptidases with a New Zinc-binding Motif

Peptidyl-Lys Metalloendopeptidase-catalyzed 18O Labeling for Comparative Proteomics

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