Purification and Characterization of Porcine Pepsinogen B and Pepsin B

Nielsen, Peter Kresten; Foltmann, Bent

doi:10.1006/abbi.1995.1483

Cited by 34 publications

(40 citation statements)

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“…However, expression of a significant amount of procathepsin E in gastric mucosa is known [34] and this is an aspartic proteinase close to pepsinogens [35], so that it could compensate for the lack of pepsinogen A. Prochymosin [36] and pepsinogen F [37] are pepsinogens specific for fetal/infant stages, as described in detail below. Pepsinogen B has been isolated only from pig [27,38]. Although it may be more widely distributed in vertebrates, it has not been studied extensively, probably because it is difficult to detect by routine assay procedures [27].…”

Section: Expression Differences and Tissue Distributionmentioning

confidence: 99%

“…The S 1 subsite of pepsin is thought to be the primary determinant of specificity, since the cleavage probability is much higher here than at any other site. Significant differences in probabil- [21,38,139], and hydrolytic activities against N-acetyl-L-phenylalanyl-L-diiodotyrosine (APDT) [19,27,93] and carbobenzoxyl-L-tyrosyl-L-leucine (ZY-L) [93] were determined at pH 2.0. The highest value in each column is taken as 100 %.…”

Section: Proteolytic Specificitymentioning

confidence: 99%

“…Apart from two different activation pathways, two different cleavage reactions are possible for activation: in- Figure 4. The primary cleavage sites upon activation of various pepsinogens are summarized based on the results of pepsinogens A from human [80,87], monkey [12,73,83], pig [74,76], cattle [142], bear [69], house musk shrew [29], rabbit [13], and chicken [81]; cattle pepsinogen B [38]; progastricsins from human [77], monkey [12,83], pig [143], house musk shrew [29], and frog [22]; cattle prochymosin [78]; and tuna pepsinogens [144]. The residues in the activation segment are numbered according to the porcine pepsinogen A sequence and characterized by the suffix p. Residues in filled boxes are conserved in these sequences.…”

Section: Zymogen Activationmentioning

confidence: 99%

“…In the case of chymosin, the secondary site is not shown because the cleavage of the bonds other than Leu15-Tyr16 was very slow. Information about the specificity of pepsin B is much less extensive than for the three enzymes described above, except that pepsin B is very active against a Phe-Tyr dipeptide (table 2) [27,38]. The specificity of pepsin F is not known.…”

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confidence: 91%

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Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development

Kageyama¹

2002

CMLS, Cell. Mol. Life Sci.

229

214

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Five types of zymogens of pepsins, gastric digestive proteinases, are known: pepsinogens A, B, and F, progastricsin, and prochymosin. The amino acid and/or nucleotide sequences of more than 50 pepsinogens other than pepsinogen B have been determined to date. Phylogenetic analyses based on these sequences indicate that progastricsin diverged first followed by prochymosin, and that pepsinogens A and F are most closely related. Tertiary structures, clarified by X-ray crystallography, are commonly bilobal with a large active-site cleft between the lobes. Two aspartates in the center of the cleft, Asp32 and Asp215, function as catalytic residues, and thus pepsinogens are classified as aspartic proteinases. Conversion of pepsinogens to pepsins proceeds autocatalytically at acidic pH by two different pathways, a one-step pathway to release the intact activation segment directly, and a stepwise pathway through a pseudo-pepsin(s). The active-site cleft is large enough to accommodate at least seven residues of a substrate, thus forming S4 through S'3 subsites. Hydrophobic and aromatic amino acids are preferred at the P1 and P'1 positions. Interactions at additional subsites are important in some cases, for example with cleavage of kappa-casein by chymosin. Two potent naturally occurring inhibitors are known: pepstatin, a pentapeptide from Streptomyces, and a unique proteinous inhibitor from Ascaris. Pepsinogen genes comprise nine exons and may be multiple, especially for pepsinogen A. The latter and progastricsin predominate in adult animals, while pepsinogen F and prochymosin are the main forms in the fetus/infant. The switching of gene expression from fetal/infant to adult-type pepsinogens during postnatal development is noteworthy, being regulated by several factors, including steroid hormones.

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Section: Expression Differences and Tissue Distributionmentioning

confidence: 99%

Section: Proteolytic Specificitymentioning

confidence: 99%

Section: Zymogen Activationmentioning

confidence: 99%

mentioning

confidence: 91%

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Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development

Kageyama¹

2002

CMLS, Cell. Mol. Life Sci.

229

214

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“…The bovine "rennet" obtained from adult animals is, in contrast, rich in pepsin and has poorer technological properties. Milk-clotting enzymes are also commercially available from other mammalian species, e.g., lamb, goat, pig (Nielsen and Foltmann 1995), or from microbial sources. All of them have found well-defined applications in the dairy industry.…”

Section: Recovery and Purification Of Mucor Spp Aspartic Proteinasesmentioning

confidence: 99%

Aspartic proteinases from Mucor spp. in cheese manufacturing

Yeğin

Fernández‐Lahore

Salgado

et al. 2010

Appl Microbiol Biotechnol

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Filamentous fungi belonging to the order of Mucorales are well known as producers of aspartic proteinases depicting milk-clotting activity. The biosynthesis level, the biochemical characteristics, and the technological properties of the resulting proteinases are affected by the producer strain and the mode of cultivation. While the milk-clotting enzymes produced by the Rhizomucor spp. have been extensively studied in the past, much less is known on the properties and potential applications of the aspartic proteinases obtained for Mucor spp. Indeed, several Mucor spp. strains have been reported as a potential source of milk-clotting enzymes having unique technological properties. Both submerged fermentation and solid substrate cultivation are proven alternatives for the production of Mucor spp. aspartic proteinases. This review provides an overview on the bioprocessing routes to obtain large amounts of these enzymes, on their structural characteristics as related to their functional properties, and on their industrial applications with focus on cheese manufacturing.

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Gastric antibacterial efficiency is different for pepsin A and C

et al. 2005

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The gastric lumen represents a bactericidal barrier, whose major components are an acidic pH and a family of isoenzymes of the gastric aspartate protease, pepsin. To evaluate whether specific pepsins are specialized in antibacterial protection, we tested their effects on the gastric pathogen Helicobacter pylori. In a recent study we found pepsin to affect the motility of the bacteria, one of its most important virulence factors. We were able to show that the antibacterial effect of pepsin occurs in two phases: rapid loss of motility and subsequent destruction. In the present study we used the rapid pepsin-induced bacterial immobilization as a marker of antibacterial efficiency. The proteolytic activity of different pepsins was normalized to values between 2 and 200 U/ml in the hemoglobin degradation test of Anson, performed at pH 2 and 5. We found that pepsin C completely inactivates H. pylori at proteolytic activities of 2 (pH 5) and 20 (pH 2) U/ml. In contrast, the activities of pepsin A and chymosin required to affect Helicobacter motility were ten times higher.

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Purification and Characterization of Porcine Pepsinogen B and Pepsin B

Cited by 34 publications

References 0 publications

Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development

Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development

Aspartic proteinases from Mucor spp. in cheese manufacturing

Gastric antibacterial efficiency is different for pepsin A and C

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