Covalent structure of bovine trypsinogen

Mikeš, O.; Tomášek, V.; Holeyšovský, V.; Šorm, F.

doi:10.1016/0304-4165(66)90182-6

Cited by 36 publications

(6 citation statements)

References 4 publications

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“…'~ Despite the large difference in concentration between that study and the present one, their spectra are in close agreement with ours. (1) 430 (0) 462 (0) 461 (1) 484 (0) 512 (1) 512 (1) 538 (1) 540 (1) 574 (1) 574 (1) 624 (1) 624 (1) 645 (1) 644 (1) 674 (0) 678 (0) 718 (1) 462 (1) 460 (1) 504 (1) 512 (1) 574 (0) 574 (0) 625 (0) 625 (1) 646 (2) 646 (2) 716 (1) 715 (0) 742 (0) 742 (0) 760 (5) 759 (3) 832 (3) 832 (3) 856 (4) 854 (5) 880 (2) 879 (2) 910 (0) 910 (0) 938 (0) 938 (0) 959 (3) 958 (2) 982 (9) 976 (6) 1007 (7) 1007 (5) 1013 (6) 1013 (4) 1040 (3) 1036 (2) 1058 (1) 1058 (1) 1085 (1) 1080 (0) 1106 (1) 1106 (0) 1130 (4) 1128 (3) 1160 (1) 1156 (0) 1180 (2) 1176 (2) 1196 (0) 1213 (5) 1213 (3) 1248 (1 0) 1243 (9) 1260 3s) 1264 (2s) 940 (5) 959 (1) 958 (0) 982 (6) 976 …”

Section: Experimental Procedures and Resultsunclassified

“…The similarities in their primary structures have long been recognized,16 and there is substantial overlap in the tertiary structures as well.'" The amino 1202 (2) 1203 (1) 1246 (9) 1240 (8) 1268 (3s) 1258 (2s) 1300 (0) 1310 (0) 1321 (1) 1340 (7) 1340 (8) 1361 (3) 1360 (3) 1395 (0) 1395 (0) 1428 (0s) 1420 (0s) 1450 (10) 1450 (10) 1461 (2s) 1461 (2s) 1496 (0) (2) 1318 (1) 1340 (8) 1338 (8) 1362 (2) 1358 (2) 1395 (1) 1389 (0) 1428 (4) 1422 (2) 1453 (10) 1452 (10) 1461 (2s) 1459 (2s) 1498 (0) 1518 (0) 1552 (6) 1551 (4) 1582 (1) Raman effect because the intensities of the Raman lines of the amino acids containing aromatic ringes are so much stronger than those of the others. On the other hand, the simjlarity in conformations should be reflected in the amide I and I11 regions and in the disulfide frequencies.…”

Section: Interpretation Of the Spectramentioning

confidence: 99%

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Laser excited Raman spectroscopy of biomolecules. 13—conformational study of α‐chymotrypsin and trypsin

Chen

Lord

1980

J Raman Spectroscopy

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The Raman spectra of bovine pancreatic a-chymotrypsin and trypsin were determined from 7% aqueous solutions and lyophilized solids containing residual sulfate ion. A large amount of P-pleated-sheet structure is presenl in both molecules, as shown by the contour of the amide 111 region, but trypsin contains substantially more a-helical conformation than does chymotrypsin. There is evidence of some change in structure of both molecules in solution as compared with the solids. The tyrosines are all or nearly all weakly hydrogen bonded in both enzymes, and the binding of sulfate ion is also weak in the lyophilized solids.

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Section: Experimental Procedures and Resultsunclassified

Section: Interpretation Of the Spectramentioning

confidence: 99%

Laser excited Raman spectroscopy of biomolecules. 13—conformational study of α‐chymotrypsin and trypsin

Chen

Lord

1980

J Raman Spectroscopy

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“…Whereas chemical homology refers to similarity in amino acid sequence (Neurath et al, 1967) conformational homology implies similarity in three-dimensional features. The well-documented chemical homology of bovine trypsin and chymotrypsin is based on their similarity in primary sequence (Walsh and Neurath, 1964;Hartley et al, 1965;Mikes et al, 1966) and on the similarity of the functional components of their active sites (Cunningham, 1965;Bender and Kaiser, 1962;Bender, 1962). Conformational homology is implied by the hypothesis that the information for three-dimensional structure is coded directly in the amino acid sequence (Epstein et al, 1963) and is supported by experimental evidence as reviewed in the introduction.…”

Section: Discussionmentioning

confidence: 99%

“…The notion that bovine trypsin and chymotrypsin have very similar tertiary structures (Neurath et al, 1967;Sigler et al, 1968) is now generally accepted. The sequences of the enzymes have been shown to be 40% homologous (Walsh and Neurath, 1964;Hartley et al, 1965;Mikes et al, 1966). Both proteins have a unique serine in an identical hexapeptide sequence that can be alkylated with DFP with concomitant loss of activity (Jansen and Balls, 1952).…”

mentioning

confidence: 99%

Immunological cross-reaction between trypsin and chymotrypsin as a guide to structural homology

Sanders¹,

Walsh²,

Arnon³

1970

Biochemistry

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“…Boxes indicate positions at which the residues are identical. The abbreviations used are DUOD, duodenase; h-CCPX, human cytotoxic cell proteinase X [21] ; h-SECT, human serine esterase from cytotoxic T-cells (human granzyme B) [22]; m-CCPI, murine granzyme B [23]; m-CCP2, murine granzyme C [24]; GLP I and GLP 11, granzyme-like proteinases I and I1 from rat duodenum [25]; RMCP I and 11, rat mast cell proteinases (chymases) I and I1 [26,151; CAT G, human cathepsin G [27]; TRP, bovine trypsin [28] ; CHT, bovine chymotrypsin A [29] ; CHTNr, chymotrypsinogen numbering.…”

Section: G L T R Y --A N T P D R L Q Q a S L P L L S N T Nmentioning

confidence: 99%

Duodenase, a New Serine Protease of Unusual Specificity from Bovine Duodenal Mucosa

Замолодчикова

Vorotyntseva

Nazimov

et al. 1995

European Journal of Biochemistry

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The complete amino acid sequence of duodenase, a new serine endopeptidase from bovine duodenal mucosa, has been determined. The sequence was reconstructed by the automated sequence analysis of the peptides obtained after cleavage with trypsin, Staphylococcus aureus V8 protease, cyanogen bromide and duodenase. The enzyme is composed of 226 amino acid residues yielding a molecular mass of 29.06 kDa. The presence of six cysteine residues and one potential sugar-chain-binding site at Asn5O was revealed. A predicted catalytic triade characteristic of the serine proteases was traced in the duodenase primary structure at the corresponding positions (His44, Asp87 and Serl81 in the sequence). Comparison of the sequence of duodenase with the other known primary structures of mammalian serine proteinases reveales the duodenase identity to granzymes from human and mice, human cathepsin G and mast cell chymases from rat, and gives an overall sequence identity of 47-55% with the mentioned enzymes. Alignment of the known serine protease and duodenase primary structures showed unique amino acid residues within the duodenase substrate-binding pocket at positions 189 (Asn) and 226 (Asp) (the bovine chymotrypsinogen A numbering). These results are discussed with respect to the relation between the duodenase unique residues within the primary specificity pocket S, and the unusual dual specificity of the enzyme.

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Covalent structure of bovine trypsinogen

Cited by 36 publications

References 4 publications

Laser excited Raman spectroscopy of biomolecules. 13—conformational study of α‐chymotrypsin and trypsin

Laser excited Raman spectroscopy of biomolecules. 13—conformational study of α‐chymotrypsin and trypsin

Immunological cross-reaction between trypsin and chymotrypsin as a guide to structural homology

Duodenase, a New Serine Protease of Unusual Specificity from Bovine Duodenal Mucosa

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