Effects of mutations in genes for proteins involved in disulphide bond formation in the periplasm on the activities of anaerobically induced electron transfer chains in

1996 ◽  
Vol 253 (1) ◽  
pp. 95 ◽  
Author(s):  
R. Metheringham ◽  
K. L. Tyson ◽  
H. Crooke ◽  
D. Missiakas ◽  
S. Raina ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Bond Formation ◽  
Disulphide Bond ◽  
Disulphide Bond Formation

Vibrio spp. secrete proaerolysin as a folded dimer without the need for disulphide bond formation

1995 ◽  
Vol 17 (6) ◽  
pp. 1035-1044 ◽  
Author(s):  
Kim R. Hardie ◽  
Angela Schulze ◽  
Michael W. Parker ◽  
J. Thomas Buckley
Keyword(s):  
Bond Formation ◽  
Disulphide Bond ◽  
Disulphide Bond Formation ◽  
Vibrio Spp

scholarly journals Influence of the peptide-chain length on disulphide-bond formation in neurohypophysial hormones and analogues

1978 ◽  
Vol 173 (2) ◽  
pp. 403-409 ◽  
Author(s):  
G Moore
Keyword(s):  
Acetic Acid ◽  
Arginine Vasopressin ◽  
Solid Phase ◽  
Bond Formation ◽  
Gel Filtration ◽  
Arginine Vasotocin ◽  
Disulphide Bond ◽  
Peptide Chain ◽  
Phase Method ◽  
Disulphide Bond Formation

(8-Arginine)vasopressin, (8-arginine)vasotocin, oxytocin and oxypressin, the ‘ring’ derivatives pressinamide and tocinamide, and the extended-chain analogues Pro-Arg-Val-(8-arginine)vasopressin and (8-arginine)vasopressinoyl-Ala-Met-Ala-NH(2), were synthesized by the solid-phase method and purified by sequential gel filtration on Sephadex G-15 in 50% acetic acid and 0.2M-acetic acid. Controlled oxidation of the thiol groups of the reduced peptides obtained after deprotection with sodium in liquid ammonia gave rise to products that depended on the length of the peptide chain: (i) nonapeptides gave monomer and dimer species, (ii) hexapeptides produced mixtures containing higher polymers, and (iii) dodecapeptides gave predominantly monomer with some dimerized material. The evidence suggests that the presence of the acyclic tail tripeptide in the nonapeptide hormones induces a conformation in the preceding hexapeptide that favours the formation of an intramolecular disulphide bond. For (8-arginine)vasopressin, intramolecular disulphide-bond formation is enhanced by extension of the peptide chain from either the N- or the C-terminus. The possible significance of these studies to neurohypophysial hormone-prohormone relationships is discussed.

Crystal structure of the DsbA protein required for disulphide bond formation in vivo

Nature ◽  
1993 ◽  
Vol 365 (6445) ◽  
pp. 464-468 ◽  
Author(s):  
Jennifer L. Martin ◽  
James C. A. Bardwell ◽  
John Kuriyan
Keyword(s):  
Crystal Structure ◽  
Bond Formation ◽  
Disulphide Bond ◽  
Disulphide Bond Formation

scholarly journals Chemical modification of Escherichia coli succinyl-CoA synthetase with the adenine nucleotide analogue 5′-p-fluorosulphonylbenzoyladenosine

1983 ◽  
Vol 215 (3) ◽  
pp. 513-518 ◽  
Author(s):  
A R S Prasad ◽  
J Ybarra ◽  
J S Nishimura
Keyword(s):  
Escherichia Coli ◽  
Catalytic Activity ◽  
Adenine Nucleotide ◽  
Bond Formation ◽  
Disulphide Bond ◽  
Thiol Groups ◽  
Binding Region ◽  
Nucleotide Analogue ◽  
Disulphide Bond Formation ◽  
Succinyl Coa Synthetase

Escherichia coli succinyl-CoA synthetase (EC 6.2.1.5) was irreversibly inactivated on incubation with the adenine nucleotide analogue 5′-p-fluorosulphonylbenzoyladenosine (5′-FSBA). Optimal inactivation by 5′-FSBA took place in 40% (v/v) dimethylformamide. ATP and ADP protected the enzyme against inactivation by 5′-FSBA, whereas desulpho-CoA, an analogue of CoA, did not. Inactivation of succinyl-CoA synthetase by 5′-FSBA resulted in total loss of almost four thiol groups per alpha beta-dimer, of which two groups appeared to be essential for catalytic activity. 5′-FSBA at the first instance appeared to interact non-specifically with non-essential thiol groups, followed by a more specific reaction with essential thiol groups in the ATP(ADP)-binding region. Plots of the data according to the method of Tsou [(1962) Sci. Sin. 11, 1535-1558] revealed that, of the two slower-reacting thiol groups, only one was essential for catalytic activity. When succinyl-CoA synthetase that had been totally inactivated by 5′-FSBA was unfolded in acidic urea and then refolded in the presence of 100 mM-dithiothreitol, 85% of the activity, in comparison with the appropriate control, was restored. These data are interpreted to indicate that inactivation of succinyl-CoA synthetase by 5′-FSBA involves the formation of a disulphide bond between two cysteine residues. Disulphide bond formation likely proceeds via a thiosulphonate intermediate between 5′-p-sulphonylbenzoyladenosine and one of the reactive thiol groups of the enzyme.

Mechanisms and catalysts of disulphide bond formation in proteins

1995 ◽  
Vol 13 (1) ◽  
pp. 18-23 ◽  
Author(s):  
Thomas E. Creighton ◽  
André Zapun ◽  
Nigel J. Darby
Keyword(s):  
Bond Formation ◽  
Disulphide Bond ◽  
Disulphide Bond Formation
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