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The prosequence of thermolysin acts as an intramolecular chaperone when expressed in trans with the mature sequence in Escherichia coli.
Marie-Claire C, Ruffet E, Beaumont A, Roques BP. Marie-Claire C, et al. Among authors: beaumont a. J Mol Biol. 1999 Feb 5;285(5):1911-5. doi: 10.1006/jmbi.1998.2449. J Mol Biol. 1999. PMID: 9925774
Thermolysin is synthesised as a pre-proenzyme, with an N-terminal prosequence of 204 residues and a mature sequence of 316 residues. ...The results show that the pro-sequence is required to obtain active thermolysin and that a covalent link with the mature se …
Thermolysin is synthesised as a pre-proenzyme, with an N-terminal prosequence of 204 residues and a mature sequence of 316 res …
Characterization of Glu350 as a critical residue involved in the N-terminal amine binding site of aminopeptidase N (EC 3.4.11.2): insights into its mechanism of action.
Luciani N, Marie-Claire C, Ruffet E, Beaumont A, Roques BP, Fournié-Zaluski MC. Luciani N, et al. Among authors: beaumont a. Biochemistry. 1998 Jan 13;37(2):686-92. doi: 10.1021/bi971705p. Biochemistry. 1998. PMID: 9425092
Given that aminopeptidases of the M1 family are likely to have a common mechanism of action, only strictly conserved residues were mutated. ...In contrast, the mutations E350Q and E350D induced a large decrease in enzyme activity, essentially due to modifications in …
Given that aminopeptidases of the M1 family are likely to have a common mechanism of action, only strictly conserved residues were mu …
The roles of the prosequence of thermolysin in enzyme inhibition and folding in vitro.
O'Donohue MJ, Beaumont A. O'Donohue MJ, et al. Among authors: beaumont a. J Biol Chem. 1996 Oct 25;271(43):26477-81. doi: 10.1074/jbc.271.43.26477. J Biol Chem. 1996. PMID: 8900115
It also inhibited a closely related enzyme produced by Bacillus stearothermophillus, albeit with a 16-fold higher IC50 value (220 nM). ...At a prosequence concentration of 5 microM a mammalian, thermolysin-like enzyme, neutral endopeptidase 24.11, was …
It also inhibited a closely related enzyme produced by Bacillus stearothermophillus, albeit with a 16-fold higher IC50 value ( …
The role of histidine 231 in thermolysin-like enzymes. A site-directed mutagenesis study.
Beaumont A, O'Donohue MJ, Paredes N, Rousselet N, Assicot M, Bohuon C, Fournié-Zaluski MC, Roques BP. Beaumont A, et al. J Biol Chem. 1995 Jul 14;270(28):16803-8. doi: 10.1074/jbc.270.28.16803. J Biol Chem. 1995. PMID: 7622493
In the zinc metallopeptidases produced by the genus Bacillus, an active site histidine has been proposed to either stabilize the transition state in catalysis by donating a hydrogen bond to the hydrated peptide (Matthews, B. ...Res. 21, 333-340) or to polarize a wat …
In the zinc metallopeptidases produced by the genus Bacillus, an active site histidine has been proposed to either stabilize the transition …
Cloning and expression in Bacillus subtilis of the npr gene from Bacillus thermoproteolyticus Rokko coding for the thermostable metalloprotease thermolysin.
O'Donohue MJ, Roques BP, Beaumont A. O'Donohue MJ, et al. Among authors: beaumont a. Biochem J. 1994 Jun 1;300 ( Pt 2)(Pt 2):599-603. doi: 10.1042/bj3000599. Biochem J. 1994. PMID: 8002967 Free PMC article.
The nucleotide sequence has revealed that, like neutral proteases produced by other members of the Bacillus species, thermolysin is probably produced as a preproenzyme carrying a typical N-terminal membrane signal sequence. Further, the thermolysin gene shares a
The nucleotide sequence has revealed that, like neutral proteases produced by other members of the Bacillus species, thermolysin is probably …
Intramolecular processing of prothermolysin.
Marie-Claire C, Roques BP, Beaumont A. Marie-Claire C, et al. Among authors: beaumont a. J Biol Chem. 1998 Mar 6;273(10):5697-701. doi: 10.1074/jbc.273.10.5697. J Biol Chem. 1998. PMID: 9488701
J., and Beaumont, A. (1996) J. Biol. Chem. 271, 26477-26481). To determine whether prosequence cleavage from the mature enzyme is autocatalytic and if so, whether it is an intermolecular or intramolecular process, N-terminal histidine-tagged prothermolysin was expre …
J., and Beaumont, A. (1996) J. Biol. Chem. 271, 26477-26481). To determine whether prosequence cleavage from the mature enzyme …
Evidence by site-directed mutagenesis that arginine 203 of thermolysin and arginine 717 of neprilysin (neutral endopeptidase) play equivalent critical roles in substrate hydrolysis and inhibitor binding.
Marie-Claire C, Ruffet E, Antonczak S, Beaumont A, O'Donohue M, Roques BP, Fournié-Zaluski MC. Marie-Claire C, et al. Among authors: beaumont a. Biochemistry. 1997 Nov 11;36(45):13938-45. doi: 10.1021/bi9712495. Biochemistry. 1997. PMID: 9374873
One active site residue of thermolysin, Arg-203, is involved in inhibitor binding by forming hydrogen bonds with the carbonyl group of a residue in the P1 position and also participates in a hydrogen bond network involving Asp-170. ...In addition, the replacement of …
One active site residue of thermolysin, Arg-203, is involved in inhibitor binding by forming hydrogen bonds with the carbonyl group of a
Irreversible photolabeling of active site of neutral endopeptidase-24.11 "enkephalinase" by azidothiorphan and [14C]-azidothiorphan.
Beaumont A, Hernandez JF, Chaillet P, Crine P, Roques BP. Beaumont A, et al. Mol Pharmacol. 1987 Nov;32(5):594-9. Mol Pharmacol. 1987. PMID: 3479679
The binding is accompanied by a loss of enzymatic activity, and the inclusion of the competitive inhibitor thiorphan protects the endopeptidase from this inactivation. ...Azidothiorphan has also been found to produce a long-lasting naloxone-reversible analgesia afte …
The binding is accompanied by a loss of enzymatic activity, and the inclusion of the competitive inhibitor thiorphan protects the end …
A 94-kDa protein, identified as neutral endopeptidase-24.11, can inactivate atrial natriuretic peptide in the vascular endothelium.
Soleilhac JM, Lucas E, Beaumont A, Turcaud S, Michel JB, Ficheux D, Fournié-Zaluski MC, Roques BP. Soleilhac JM, et al. Among authors: beaumont a. Mol Pharmacol. 1992 Apr;41(4):609-14. Mol Pharmacol. 1992. PMID: 1533267
The presence of the 94-kDa neutral endopeptidase in rabbit aortic tissue was definitively established using a new potent 125I-labeled inhibitor, [125I]RB104 [2-[(3-[125I]iodo-4-hydroxy)phenylmethyl]-4-N-[3- hydroxyamino-3-oxo-1-phenylmethyl propyl]amino-4-oxobutanoic acid] …
The presence of the 94-kDa neutral endopeptidase in rabbit aortic tissue was definitively established using a new potent 125I-labeled …
Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology.
Roques BP, Noble F, Daugé V, Fournié-Zaluski MC, Beaumont A. Roques BP, et al. Among authors: beaumont a. Pharmacol Rev. 1993 Mar;45(1):87-146. Pharmacol Rev. 1993. PMID: 8475170 Review. No abstract available.
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