Erratum: The kinetics of inactivation of adenylosuccinate lyase: evidence for a substrate-induced conformational change

1969 ◽  
Vol 47 (9) ◽  
pp. 898-899
Author(s):  
W. A. Bridger ◽  
L. H. Cohen
Keyword(s):  
Conformational Change ◽  
Adenylosuccinate Lyase ◽  
Kinetics Of

The kinetics of inactivation of adenylosuccinate lyase: evidence for a substrate-induced conformational change

1969 ◽  
Vol 47 (6) ◽  
pp. 665-672 ◽  
Author(s):  
W. A. Bridger ◽  
L. H. Cohen
Keyword(s):  
Kinetic Study ◽  
Conformational Change ◽  
Initial Rate ◽  
Alkylating Agents ◽  
Free Enzyme ◽  
The Other ◽  
Adenylosuccinate Lyase ◽  
Product Release ◽  
Rate Kinetics ◽  
Kinetics Of

The kinetics of inactivation of adenylosuccinate lyase by the alkylating agents N-ethyl maleimide and iodoacetamide and by photooxidation have been investigated. The inactivation by the alkylating agents indicates that there are several groups on the enzyme whose reaction affects activity. The presence of AMP, a product of the enzymic reaction, decreases the rate of inactivation by both N-ethyl maleimide and iodoacetamide, while the other product, fumarate, has no effect on the rate. In the case of photoinactivation, the rate is accelerated by the presence of AMP. Fumarate, which again has no effect by itself, causes an overall protection of the enzyme from photoinactivation when added in the presence of AMP. The results, suggesting that fumarate is unable to combine with the free enzyme but does combine with the enzyme–AMP complex, are consistent with the strongly preferred sequence of product release determined by a previous initial-rate kinetic study. Both the kinetics of inactivation and the initial-rate kinetics may be interpreted in terms of a mechanism involving the operation of an enzymic conformational change which is allowed only when either AMP or adenylosuccinate is bound to the enzyme.

scholarly journals Positive co-operative binding at two weak lysine-binding sites governs the Glu-plasminogen conformational change

1992 ◽  
Vol 285 (2) ◽  
pp. 419-425 ◽  
Author(s):  
U Christensen ◽  
L Mølgaard
Keyword(s):  
Ligand Binding ◽  
Binding Site ◽  
Conformational Change ◽  
Conformational Changes ◽  
Binding Sites ◽  
High Specificity ◽  
Stopped Flow ◽  
Protein Fluorescence ◽  
Lysine Residues ◽  
Kinetics Of

The kinetics of a series of Glu-plasminogen ligand-binding processes were investigated at pH 7.8 and 25 degrees C (in 0.1 M-NaCl). The ligands include compounds analogous to C-terminal lysine residues and to normal lysine residues. Changes of the Glu-plasminogen protein fluorescence were measured in a stopped-flow instrument as a function of time after rapid mixing of Glu-plasminogen and ligand at various concentrations. Large positive fluorescence changes (approximately 10%) accompany the ligand-induced conformational changes of Glu-plasminogen resulting from binding at weak lysine-binding sites. Detailed studies of the concentration-dependencies of the equilibrium signals and the rate constants of the process induced by various ligands showed the conformational change to involve two sites in a concerted positive co-operative process with three steps: (i) binding of a ligand at a very weak lysine-binding site that preferentially, but not exclusively, binds C-terminal-type lysine ligands, (ii) the rate-determining actual-conformational-change step and (iii) binding of one more lysine ligand at a second weak lysine-binding site that then binds the ligand more tightly. Further, totally independent initial small negative fluorescence changes (approximately 2-4%) corresponding to binding at the strong lysine-binding site of kringle 1 [Sottrup-Jensen, Claeys, Zajdel, Petersen & Magnusson (1978) Prog. Chem. Fibrinolysis Thrombolysis 3, 191-209] were observed for the C-terminal-type ligands. The finding that the conformational change in Glu-plasminogen involves two weak lysine-binding sites indicates that the effect cannot be assigned to any single kringle and that the problem of whether kringle 4 or kringle 5 is responsible for the process resolves itself. Probably kringle 4 and 5 are both participating. The involvement of two lysine binding-sites further makes the high specificity of Glu-plasminogen effectors more conceivable.

Kinetics of Conformational Change of Troponin C Induced by Calcium1

1976 ◽  
Vol 79 (3) ◽  
pp. 689-691 ◽  
Author(s):  
Takayoshi IIO ◽  
Koshin MIHASHI ◽  
Hiroshi KONDO
Keyword(s):  
Conformational Change ◽  
Troponin C ◽  
Kinetics Of

scholarly journals 1P439 Kinetics of major conformational change of PYP(17. Light driven system,Poster Session,Abstract,Meeting Program of EABS &BSJ 2006)

2006 ◽  
Vol 46 (supplement2) ◽  
pp. S256
Author(s):  
Yuji Hoshihara ◽  
Yasushi Imamoto ◽  
Mikio Kataoka ◽  
Fumio Tokunaga ◽  
Yoshifumi Kimura ◽  
...  
Keyword(s):  
Conformational Change ◽  
Poster Session ◽  
Meeting Program ◽  
Driven System ◽  
Kinetics Of
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