Antipain inhibits thyroxine-induced synthesis of carbamyl phosphate synthetase I in tadpole liver.

Mori, Masataka; Cohen, Philip P.

doi:10.1073/pnas.75.11.5339

Cited by 12 publications

(2 citation statements)

References 26 publications

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“…Chymostatin and synthetic analogues have been investigated for therapeutic potency. Control of enzyme activation by inhibition of the processing proteases − as well as prevention of protein degradation, as may occur with liver and skeleton muscle proteins, may be beneficial in certain diseases. The synthesis of tyrosine-containing chymostatin derivatives has not been reported, and dipeptides and tripeptides did not show better activity than that of the bacterial chymostatins .…”

Section: Discussionmentioning

confidence: 99%

Decoding the Papain Inhibitor from Streptomyces mobaraensis as Being Hydroxylated Chymostatin Derivatives: Purification, Structure Analysis, and Putative Biosynthetic Pathway

et al. 2020

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Streptomyces mobaraensis produces the papain inhibitor SPI consisting of a 12 kDa protein and small active compounds (SPI ac ). Purification of the papain inhibitory compounds resulted in four diverse chymostatin derivatives that were characterized by NMR and MS analysis. Chymostatins are hydrophobic tetrapeptide aldehydes from streptomycetes, e.g., S. lavendulae and S. hygroscopicus, that reverse chymosin-mediated angiotensin activation and inhibit other serine and cysteine proteases. Chymotrypsin and papain were both inhibited by the SPI ac compounds in the low nanomolar range. SPI ac differs from the characterized chymostatins by the exchange of phenylalanine for tyrosine. The crystal structure of one of these chymostatin variants confirmed its molecular structure and revealed a S-configured hemithioacetal bond with the catalytic Cys25 thiolate as well as close interactions with hydrophobic S1 and S2 subsite amino acids. A model for chymostatin biosynthesis is provided based on the discovery of clustered genes encoding several putative nonribosomal peptide synthetases; among them, there is the unusual CstF enzyme that accommodates two canonical amino acid activation domains as well as three peptide carrier protein domains.

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Section: Discussionmentioning

confidence: 99%

Decoding the Papain Inhibitor from Streptomyces mobaraensis as Being Hydroxylated Chymostatin Derivatives: Purification, Structure Analysis, and Putative Biosynthetic Pathway

et al. 2020

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“…At the end of an 8-h labelling period, the liver was removed and leucine incorporation into total protein of the liver was measured [26].…”

Section: ''C-labelled Leucine Incorporrrtion Studiesmentioning

confidence: 99%

Regulation of N‐Acetylglutamate Synthetase in Mouse Liver

Kawamoto

Ishida

Mori

et al. 1982

European Journal of Biochemistry

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N-Acetyl-L-glutamate synthetase catalyzes the synthesis of N-acetyl-L-glutamate, an allosteric and essential activator of carbamoyl-phosphate synthetase I in the liver of ureotelic animals. The enzyme is activated specifically by arginine.1. Mice were fed laboratory chow (protein content, 21 x) for 3 h and, after various times, N-acetyl-L-glutamate synthetase activity in the sonicated mitochondria was measured both in the presence and absence of 1 niM L-arginine. The activity in the absence of arginine did not significantly change after the feeding, while the activity in the presence of arginine increased with time and reached a maximum (fivefold increase) 9 h after the start of feeding, then decreased gradually. The ratio of the activity with arginine to that without arginine was 1.6 at the start of feeding and 5.5 at 9 h.2. Similar postprandial changes were observed with the mice on a protein-free diet, when these mice had previously been on a protein diet. No such change was seen with a protein-free diet when the mice were previously given a protein-free diet for a few days.3. Cycloheximide injection, which inhibited the total protein synthesis in the mouse liver by 90%, did not inhibit the postprandial increase in arginine activation of the synthetase. Thus, protein synthesis is presumably not required for the change.4. The enzymes with a low and a high arginine sensitivity were purified over tenfold from mitochondrial extracts of fasted and fed animals respectively. The extent of arginine activation of the enzymes remained unchanged, low or high, throughout the purification. In Sephacryl S-300 chromatography both types of the enzyme were eluted as a single peak and corresponded to a M, of 220000-250000. The change in arginine activation may be due to a modification of the enzyme molecule without a gross change in the molecular weight. 5. The diet-dependent change in sensitivity of the synthetase to arginine presents a new type of regulation of this enzyme and this regulation may contribute to the prevention of a rapid decrease in hepatic acetylglutamate levels after food ingestion N-Acetyl-L-glutamate is a specific and obligatory allosteric activator of mitochondrial carbamoyl-phosphate synthetase

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Cell death in metamorphosis

Lockshin¹

1981

Cell Death in Biology and Pathology

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Antipain inhibits thyroxine-induced synthesis of carbamyl phosphate synthetase I in tadpole liver.

Cited by 12 publications

References 26 publications

Decoding the Papain Inhibitor from Streptomyces mobaraensis as Being Hydroxylated Chymostatin Derivatives: Purification, Structure Analysis, and Putative Biosynthetic Pathway

Decoding the Papain Inhibitor from Streptomyces mobaraensis as Being Hydroxylated Chymostatin Derivatives: Purification, Structure Analysis, and Putative Biosynthetic Pathway

Regulation of N‐Acetylglutamate Synthetase in Mouse Liver

Cell death in metamorphosis

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