The complete amino acid sequence of prochymosin.

Foltmann, Bent; Pedersen, Vibeke Barkholt; Jacobsen, Henning; Kauffman, Dorothy L.; Wybrandt, Grith B.

doi:10.1073/pnas.74.6.2321

Cited by 91 publications

(25 citation statements)

References 31 publications

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“…The aspartic acids at the active sites of acid proteases are marked with asterisks. References for sequence data used: human (Sogawa et al, 1983), porcine (Tang et al, 1973) and bovine (Harboe and Foltmann, 1975) pepsinogen; bovine prochymosin (Foltmann et al, 1977); penicillopepsin (Hsu et al, 1977); renin from mouse (Panthier et al, 1982) and human (Hobart et al, 1984).…”

Section: Resultsmentioning

confidence: 99%

Close structural resemblance between putative polymerase of a Drosophila transposable genetic element 17.6 and pol gene product of Moloney murine leukaemia virus.

Toh¹,

Kikuno²,

Hayashida³

et al. 1985

The EMBO Journal

158

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We have made a computer-assisted search for homology among polymerases or putative polymerases of various viruses and a transposable element, the Drosophila copia-like element 17.6. The search revealed that the putative polymerase (second open reading frame) of the copia-like element 17.6 bears close resemblance in overall structural organization to the pol gene product of Moloney murine leukaemia virus (M-MuLV): they show significant homology to each other at both the Nand C-terminal portions, suggesting that the 17.6 putative polymerase carries two enzymatic activities, related to reverse transcriptase and DNA endonuclease. The putative polymerase of cauliflower mosaic virus (CaMV) shows striking homology with the putative polymerase of 17.6 over almost its entire length, but it lacks the DNA endonuclease-related sequence. Furthermore, it was shown that the N-terminal ends of the M-MuLV pol product and the CaMV and 17.6 putative polymerases exhibit strong sequence homology with the gag-specific protease (p15) of Rous sarcoma virus (RSV) as well as the amino acid sequence predicted from the gag/pol spacer sequence of human adult T-celi leukaemia virus (HTLV). These p15-related sequences contain a highly conserved stretch of amino acids which show a close similarity with sequences around the active site amino acids Asp-ThrGly of the acid protease family, suggesting that they have an activity similar to acid protease. On the basis of the alignment of reverse transcriptase-related sequences, a dendrogram representing phylogenetic relationships among all the viruses compared together with 17.6 was constructed and its evolutionary implication is discussed.

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Section: Resultsmentioning

confidence: 99%

Close structural resemblance between putative polymerase of a Drosophila transposable genetic element 17.6 and pol gene product of Moloney murine leukaemia virus.

Toh¹,

Kikuno²,

Hayashida³

et al. 1985

The EMBO Journal

158

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“…The sequence ofproteinase A is compared to the known primary structures of porcine cathepsin D (44), human renin (21), porcine pepsin (43), bovine chymosin (13) and penicillopepsin (22), with emphasis on residues corresponding to catalytically and structurally important residues in the enzymes with known three-dimensional structure.…”

Section: Introductionmentioning

confidence: 99%

Primary structure of the aspartic proteinase A from Saccharomyces cerevisiae

Dreyer

Halkier

Svendsen

et al. 1986

Carlsberg Res. Commun.

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Proteinase A was purified by an improved large scale procedure and split into fragments by means of trypsin, cyanogen bromide, hydroxylamine, and o-iodosobenzoic acid. On the basis of high degrees of homology with cathepsin D and pepsin its amino acid sequence was determined. Proteinase A contains 329 amino acid residues, and in addition 8.5% neutral sugar and 1% glucosamine, attached to asparagines in positions 67 and 267. Proteinase A contains two disulfide bonds, as opposed to three in mammalian aspartic proteinases. Comparison with the tertiary structure of pepsin indicates, that the two catalytically essential aspartic acid residues, and the residues corresponding to their surroundings, are conserved. The sequence shows 46% identity with porcine cathepsin D and 40% with porcine pepsin. An aspartic proteinase from Saccharomyces carlsbergensis had the same N-terminal 40 amino acid sequence as proteinase A. Immunological cross-reactivity between proteinase A and calfchymosin was demonstrated by immune blotting assay.

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“…Other aspartyl proteases, such as pepsin and chymosin, are processed from an inactive precursor with the release of a prosegment to give active enzymes (5)(6)(7). Furthermore, the recent elucidation of the structural gene coding for human pepsin has shown that the pepsin precursor also contains a 15-amino acid signal peptide and a 47-amino acid activation segment (8).…”

mentioning

confidence: 99%

Synthesis of peptides related to the prosegment of mouse submaxillary gland renin precursor: an approach to renin inhibitors.

Evin¹,

Devin²,

Castro³

et al. 1984

Proc. Natl. Acad. Sci. U.S.A.

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The complete sequence of the structural gene coding for mouse submaxillary gland renin was recently reported and the amino acid sequence of preprorenin was deduced. This sequence includes a 45-amino acid peptide that corresponds to the prosegment of the renin precursor. To investigate whether peptides related to the renin prosegment are able to inhibit renin activity, we have synthesized four peptides having the following structures: Arg-Ile-Pro-OMe, butyloxycarbonyl(Boc)-Leu-Lys-Lys-Met-Pro-OMe, Boc-Arg-Ile-ProLeu-Lys-Lys-Met-Pro-OMe, and Boc-Glu-Arg-Ile-Pro-LeuLys-Lys-Met-Pro-OMe (corresponding to amino acids 12-14, L-19, 12-19, and 11-19, respectively, of the renin prosegment). All four peptides were found to inhibit the activity of pure mouse submaxillary renin on a porcine synthetic tetradecapeptide in vitro, and the most potent inhibitors exhibited ICso values in the micromolar range. Enzymatic kinetic studies carried out using peptide 15-19 showed an uncompetitive or a mixed type of inhibition with a Ki value of 2.3 x 10-6 M at 37°C in 0.5 M citrate/phosphate buffer (pH 6.0).Renin plays an important role in the regulation of blood pressure and electrolyte metabolism (1). It is a very specific aspartyl protease that reacts with its substrate angiotensinogen to release angiotensin I. Mouse submaxillary gland renin has physicochemical, enzymatic, and immunological properties similar to those of the renal enzyme (2, 3). The complete sequence of the structural gene coding for mouse submaxillary renin has been reported by Panthier et al., and the amino acid sequence of preprorenin was deduced (4). A hypothesis for renin processing consisting of a three-step mechanism has been proposed (4): (i) the removal of a signal peptide leading to prorenin, (ii) the cleavage of an NH2-terminal activation peptide later referred to as the prosegment, (iii) the splitting of the renin molecule into two chains linked by a disulfide bond to give the mature active enzyme. The exact length of the signal peptide could not be determined, but by analogy with the signal peptides of other proteins, an 18-amino acid peptide (-18 to -1) was proposed by Panthier et al. (4). Consequently, the prosegment of prorenin was proposed to be a 45-amino acid peptide (1-45).Other aspartyl proteases, such as pepsin and chymosin, are processed from an inactive precursor with the release of a prosegment to give active enzymes (5-7). Furthermore, the recent elucidation of the structural gene coding for human pepsin has shown that the pepsin precursor also contains a 15-amino acid signal peptide and a 47-amino acid activation segment (8). In all cases the prosegments are located at the NH2 terminus and have a length comparable to that of the putative renin prosegment. A notable homology has been found in the prosegment sequences of the renin precursor and of pepsinogen, particularly in the NH2-terminal region (Fig. 1).Interestingly, the enzymatic activities of bovine and porcine pepsins are inhibited by peptide fragments from the prosegments of ...

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The complete amino acid sequence of prochymosin.

Cited by 91 publications

References 31 publications

Close structural resemblance between putative polymerase of a Drosophila transposable genetic element 17.6 and pol gene product of Moloney murine leukaemia virus.

Close structural resemblance between putative polymerase of a Drosophila transposable genetic element 17.6 and pol gene product of Moloney murine leukaemia virus.

Primary structure of the aspartic proteinase A from Saccharomyces cerevisiae

Synthesis of peptides related to the prosegment of mouse submaxillary gland renin precursor: an approach to renin inhibitors.

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