On the Proteolytic Enzymes of Animal Tissues

Fruton, Joseph S.; Smith, Virginia A.; Driscoll, Peter

doi:10.1016/s0021-9258(18)57417-2

Cited by 48 publications

(6 citation statements)

References 12 publications

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“…is anatomically ubiquitous in man and other animals, having been characterized from brain (Hui & Lajtha, 1978), erythrocytes (Endo et al, 1982), heart (Smith, 1948), intestinal mucosa (Rubino et al, 1969), kidney (Davis & Smith, 1957), leukocytes (Powell et al, 1974), liver (Norén et al, 1977), 0006-2960/86/0425-1054$01.50/0 © 1986 American Chemical Society plasma (Myara et al, 1984a), skin fibroblasts (Sheffield et al, 1977), thymus (Fruton et al, 1948), and the uterus (Smith, 1948). A rare congenital abnormality in man known as prolidase deficiency, in which there is a complete absence of the enzyme, manifests itself as a general clinical syndrome which includes splenomegaly, chronic ulcerative dermatitis, recurrent respiratory tract infection, mild to moderately severe mental retardation, and massive imidodipeptiduria [for a review, see Kaloustian et al (1982)].…”

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confidence: 99%

Direct NMR evidence that prolidase is specific for the trans isomer of imidodipeptide substrates

King¹,

Middlehurst²,

Kuchel³

1986

Biochemistry

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The in vitro hydrolysis by porcine kidney prolidase of the imidodipeptide L-alanyl-L-proline was monitored by using 1H high-resolution NMR spectroscopy. The dipeptide exists as an equilibrium mixture of isomers with cis or trans conformation about the peptide bond. The 13C and 1H NMR spectra of the dipeptide displayed well-resolved resonances for each isomer. Inversion-transfer NMR spectroscopy, with a recently developed pulse sequence, was used with a range of temperatures to calculate the unitary rate constants for the exchange between isomers. A new analytical procedure was introduced for directly obtaining estimates of the unitary rate constants from inversion-transfer data. Arrhenius analysis yielded an activation energy for the isomerization of 87.0 +/- 4.1 kJ mol-1. 1H NMR time courses of the prolidase-catalyzed hydrolysis of L-alanyl-L-proline showed a faster removal of the trans isomer as the [enzyme]/[substrate] ratio was increased. The transient-kinetic information coupled with the steady-state kinetic parameters of the enzyme was used to develop two possible models of the overall hydrolytic reaction. Numerical integration of the relevant differential equations using the experimentally determined rate constants gave simulated progress curves that enabled selection of one of the proposed schemes as being the most likely; this proposal entailed absolute specificity of prolidase for the trans isomer of L-alanyl-L-proline. Finally, on the basis of the present work, and information from the literature, we have proposed a new model of the active site of the enzyme.

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confidence: 99%

Direct NMR evidence that prolidase is specific for the trans isomer of imidodipeptide substrates

King¹,

Middlehurst²,

Kuchel³

1986

Biochemistry

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“…The aminopeptidase activity is stable for months when stored frozen or refrigerated under toluene. However, dipeptidase activity is lost on storage for long periods and may be more susceptible to inactivation by aging (Robinson & Shaw, 1960;Smith, 1948) and by some purification procedures (Bergmann & Smith, 1941). Tetraglycine is not cleaved by the enzyme preparations.…”

Section: Discussionmentioning

confidence: 99%

“…Tetraglycine is not cleaved by the enzyme preparations. Since only very slight hydrolysis of tetrapeptides consisting of at least three glycine residues has been reported by Fruton et al (1948) in studies on an aminotripeptidase, and by with leucine aminopeptidase, it appears that such tetrapeptides are less susceptible than diand tri-peptides to hydrolysis by aminopeptidases.…”

Section: Discussionmentioning

confidence: 99%

“…Some physical and chemical characteristics of the metal-ion-requiring leucine aminopeptidase derived from kidney cortex have been investigated (Spackman, Smith & Brown, 1955;. A peptidase not requiring metal ions in calf thymus has also been described (Fruton, Smith & Driscoll, 1948). Aminopeptidases and dipeptidases have been reported to be widely distributed in mammalian organs and body fluids, and have been found to vary greatly in substrate specificity and in metal ion requirements.…”

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Studies on ox brain aminopeptides

Brecher

Sobel

1967

Biochemical Journal

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1. Mn(2+)-inhibited and Mn(2+)-activated aminopeptidases have been observed in ox brain and separated from one another by DEAE-cellulose column chromatography. 2. The Mn(2+)-inhibited enzyme has been purified 36-fold; it exhibits a specificity for tripeptide substrates, whereas the Mn(2+)-activated aminopeptidase cleaves dipeptides as well as tripeptides. 3. Ammonium sulphate treatment generates a Mn(2+)-stimulated aminopeptidase that is stable to dialysis against EDTA and water, in contrast with an endogenous Mn(2+)-activated preparation that is irreversibly denatured by such dialysis against EDTA and water.

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“…Ή λευκινοαμινοπεπτιδάση, μη είδικον πρωτεολυτικον 13 , 14 ενζυμον 20 , ανήκει εις τάς έξωπεπτιδάσας 61 και ύδρολύει κυρίως πεπτίδια φέροντα λευκίνην μετά ελευθέρας άμινικής ομάδος. 1 ) έξωηπατικήν άπόφραξιν των χοληφόρων οδών.…”

Section: γενικον μεροςunclassified

Λευκινοαμινοπεπτιδαση Ορου Αιματος Και Ισοενζυμα Αυγης Επι Ηπατιτιδος Παιδιων

Αρωνη¹

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On the Proteolytic Enzymes of Animal Tissues

Cited by 48 publications

References 12 publications

Direct NMR evidence that prolidase is specific for the trans isomer of imidodipeptide substrates

Direct NMR evidence that prolidase is specific for the trans isomer of imidodipeptide substrates

Studies on ox brain aminopeptides

Λευκινοαμινοπεπτιδαση Ορου Αιματος Και Ισοενζυμα Αυγης Επι Ηπατιτιδος Παιδιων

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