Specificity and inhibition studies of Armillaria mellea protease

Lewis, William; Basford, J. M.; Walton, Peter L.

doi:10.1016/0005-2744(78)90087-6

Cited by 47 publications

(15 citation statements)

References 16 publications

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“…34,[42][43][44][45] Noteworthy, the pattern of SDF-1␣ cleavage at the COOH terminus and metal dependency of the reaction bear similarity to the characteristics of Armillaria mellea protease, a metalloenzyme that can work close to the termini of polypeptide chains and displays primary specificity toward peptide bonds where a lysine residue contributes an ␣ amino group. 46,47 Studies of the structural basis for SDF-1␣ biologic activity have failed to reveal a role for the COOH domain. However, it is worth noting that such studies have utilized the SDF-1␣ 1-67 variant, which lacks the carboxy-terminal lysine.…”

Section: Discussionmentioning

confidence: 99%

Differential processing of stromal-derived factor-1α and stromal-derived factor-1β explains functional diversity

Sierra

Yang²,

Narazaki³

et al. 2004

Blood

191

109

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The chemokine stromal-derived factor-1 (SDF-1), which is constitutively expressed in most tissues as SDF-1alpha and SDF-1beta resulting from alternative gene splicing, regulates hematopoiesis, lymphocyte homing, B-lineage cell growth, and angiogenesis. Because SDF-1alpha and SDF-1beta are constitutively and ubiquitously expressed, their degradation must serve an important regulatory role. Here we show that SDF-1alpha and SDF-1beta are secreted as full-length molecules. When exposed to human serum, full-length SDF-1alpha (1-68) undergoes processing first at the COOH terminus to produce SDF-1alpha 1-67 and then at the NH2 terminus to produce SDF-1alpha 3-67. By contrast, full-length SDF-1beta (1-72) is processed only at the NH2 terminus to produce SDF-1beta 3-72. CD26/dipeptidyl peptidase is responsible for serum cleavage of SDF-1alpha and SDF-1beta at the NH2 terminus. Serum processing of SDF-1alpha at the COOH terminus, which has not been previously reported, reduces the ability of the polypeptide to bind to heparin and to cells and to stimulate B-cell proliferation and chemotaxis. The additional processing at the NH2 terminus renders both forms of SDF-1 unable to bind to heparin and to activate cells. The differential processing of SDF-1alpha and SDF-1beta provides biologic significance to the existence of 2 splice forms of the chemokine and adds a tool to precisely regulate SDF-1's biologic activity by changes in specific activity.

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Section: Discussionmentioning

confidence: 99%

Differential processing of stromal-derived factor-1α and stromal-derived factor-1β explains functional diversity

Sierra

Yang²,

Narazaki³

et al. 2004

Blood

191

109

View full text Add to dashboard Cite

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“…Wittmann samples of protein L17 and Dr for providing V. BarkholtSearching of homologous sequence stretches was made by the aid of a computer programme for different length (8, 10,12,14,16,20, 24 and 30 residues). The accuracy was set to 3550% identities among the two proteins compared; and of the remaining non-identical amino acids at least 35% had related codons differing in one or two nucleotides: (a) identical residues; (+) amino acids whose codons differ by 1 nucleotide; (-) amino acids Pedersen for a gift of Armillaria mellea protease.…”

Section: Acknowledgementsmentioning

confidence: 99%

The primary structure of protein L17 from the Escherichia coli ribosome

1982

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The complete sequence of protein L17 which is a component of the large subunit of the E. coli ribosome has been determined. Peptides deriving from enzymatic hydrolysis with trypsin, thermolysin, chymotrypsin and S. aureus and A. mellea protease were isolated and sequenced by the DABITWPITC double coupling method. Some overlapping peptides were obtained after mild acid cleavage of the protein. According to the amino acid sequence protein L17 contains 127 residues and has a molecular mass of 14 365. The primary structure of protein L17 agrees well with the amino acid analysis of the intact protein and its Nterminal sequence as derived from automatic sequencing in an improved Beckman sequencer. Secondary predictions and a search for homologous sequence stretches to other ribosomal proteins were made. E. coli ribosome Protein L17Primary structure determination Secondary structure predictions

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“…The peptide fragments were identified by amino acid composition (Table 2) the primary specificity of the enzyme is considered to be cleavage at the N-terminal side of lysine residues (Lewis et al, 1978), cleavage at the N-terminal side of the arginine residue at position 8 in the substrate was observed. In a previous study in which aspartate aminotransferase was digested with the enzyme, cleavage was seen at the site of three arginine residues (Doonan et al, 1975).…”

Section: Discussionmentioning

confidence: 99%

Characterization of three peptides derived from prosomatostatin [prosomatostatin-(1–63)-, -(65–76)- and -(79–92)-peptides] in a human pancreatic tumour

Conlon

Eriksson

Grimelius

et al. 1987

Biochemical Journal

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By using only reverse-phase h.p.l.c., three fragments of prosomatostatin were isolated from an extract of a human pancreatic neuroendocrine tumour that produced somatostatin, vasoactive intestinal polypeptide and gastrin-releasing peptide. The amino acid composition of the peptides indicated that they represented prosomatostatin-(1-63)-peptide, prosomatostain-(65-76)-peptide and prosomatostatin-(79-92)-peptide (somatostatin-14). The identity of prosomatostatin-(1-63)-peptide was confirmed by characterization of the products of digestion with Armillaria mellea (honey fungus) proteinase. Partial micro-sequencing of prosomatostatin-(1-63)-peptide showed that the Gly24-Ala25 bond of preprosomatostatin was the site of cleavage of the signal peptide. Thus human prosomatostatin is a protein of 92 amino acid residues that is proteolytically cleaved in a pancreatic tumour at the site of a dibasic-residue (arginine-lysine) processing site and at a single-monobasic-residue (arginine) processing site.

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Specificity and inhibition studies of Armillaria mellea protease

Cited by 47 publications

References 16 publications

Differential processing of stromal-derived factor-1α and stromal-derived factor-1β explains functional diversity

Differential processing of stromal-derived factor-1α and stromal-derived factor-1β explains functional diversity

The primary structure of protein L17 from the Escherichia coli ribosome

Characterization of three peptides derived from prosomatostatin [prosomatostatin-(1–63)-, -(65–76)- and -(79–92)-peptides] in a human pancreatic tumour

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