Über eine neue <i>l</i>‐Aminosäure‐oxydase. (1. Mitteilung)

Zeller, E. A.; Maritz, A.

doi:10.1002/hlca.194402701241

Cited by 82 publications

(10 citation statements)

References 17 publications

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“…L-amino acid oxidases, in contrast to D-amino acid oxidases (DAAOs), possess a latent toxicity which fits their occurrence in nature: the first LAAOs described 15 were part of snake venoms. For this reasons the LAAOs from snake venoms are the best investigated representatives of this class of enzymes.…”

mentioning

confidence: 96%

The Structure of a Bacterial l-Amino Acid Oxidase from Rhodococcus opacus Gives New Evidence for the Hydride Mechanism for Dehydrogenation

Faust

Niefind

Hummel

et al. 2007

Journal of Molecular Biology

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mentioning

confidence: 96%

The Structure of a Bacterial l-Amino Acid Oxidase from Rhodococcus opacus Gives New Evidence for the Hydride Mechanism for Dehydrogenation

Faust

Niefind

Hummel

et al. 2007

Journal of Molecular Biology

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“…In the method the snake venom amino acid does not interact with the peptide substrates (Zeller & Maritz, 1944). The lack of interference by substrates coupled with the high intrinsic sensitivity of the method makes it suitable for kinetic studies of peptidase activity.…”

Section: Introductionmentioning

confidence: 99%

Oligopeptidases of brush border membranes of rat small intestinal mucosal cells

Fujita¹,

Parsons²,

Wojnarowska³

1972

The Journal of Physiology

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SUMMARY1. The properties of peptidases located in the brush borders of rat small intestinal mucosal cells have been investigated using a new method for the assay of peptidase activity. In this method amino acids produced by hydrolysis of peptides are oxidized by ophidian L-amino acid oxidase and the hydrogen peroxide produced during reoxidation of the reduced enzyme is estimated spectrophotometrically.2. 10-20 % of the total cellular peptidase activity and 50 % of the leucylnaphthylamidase (LNAase) activity were found to be tightly bound to the brush borders and to possess different substrate specificity from the supernatant peptidase activity.3. Evidence from kinetic and competition studies indicates the presence of more than one peptidase in the brush borders. The peptidases exhibit pH optima of 8-0-8-5, are inhibited by EDTA, but are not usually activated by divalent metal ions. The brush border peptidases hydrolyse di-and tripeptides, some oligopeptides, leucinamide and leucyl-,fnaphthylamine. On the basis of the Michaelis constants, these substrates differ in their affinities for the enzymes.4. It is proposed that the brush border peptidases serve an analogous function in the terminal stages of protein digestion to that of the disaccharidases in the case of carbohydrate digestion and absorption.

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“…Snake venoms were chosen as sources of L-amino acid oxidases (Zeller & Maritz, 1944). Dried venoms from various species were kindly provided by the late Dr C. H. Kellaway and tested for activity.…”

Section: Preparation Of Enzymnesmentioning

confidence: 99%