scholarly journals Characterization of Nicotinamidases: Steady State Kinetic Parameters, Classwide Inhibition by Nicotinaldehydes, and Catalytic Mechanism

Biochemistry ◽  
2010 ◽  
Vol 49 (49) ◽  
pp. 10421-10439 ◽  
Author(s):  
Jarrod B. French ◽  
Yana Cen ◽  
Tracy L. Vrablik ◽  
Ping Xu ◽  
Eleanor Allen ◽  
...  
Keyword(s):  
Steady State ◽  
Kinetic Parameters ◽  
Catalytic Mechanism ◽  
Steady State Kinetic ◽  
State Kinetic

scholarly journals Steady state kinetic parameters for the thrombin-catalyzed conversion of human fibrinogen to fibrin.

1983 ◽  
Vol 258 (15) ◽  
pp. 9276-9282 ◽  
Author(s):  
D L Higgins ◽  
S D Lewis ◽  
J A Shafer
Keyword(s):  
Steady State ◽  
Kinetic Parameters ◽  
Human Fibrinogen ◽  
Steady State Kinetic ◽  
State Kinetic

scholarly journals Variation in the Steady State Kinetic Parameters of Wild Type and Mutant T5 5′-3′-Exonuclease With pH

1999 ◽  
Vol 274 (25) ◽  
pp. 17711-17717 ◽  
Author(s):  
Timothy J. Pickering ◽  
Scott Garforth ◽  
Jon R. Sayers ◽  
Jane A. Grasby
Keyword(s):  
Steady State ◽  
Kinetic Parameters ◽  
Wild Type ◽  
Steady State Kinetic ◽  
State Kinetic

Steady state kinetic parameters of bulk V2O5 for ethane and propane oxidation reactions

2007 ◽  
Vol 8 (6) ◽  
pp. 957-962 ◽  
Author(s):  
T.V. Malleswara Rao ◽  
Goutam Deo
Keyword(s):  
Steady State ◽  
Kinetic Parameters ◽  
Propane Oxidation ◽  
Oxidation Reactions ◽  
Steady State Kinetic ◽  
State Kinetic

Catalytic mechanism of KDO8P synthase. Pre-steady-state kinetic analysis using rapid chemical quench flow methods

1997 ◽  
Vol 7 (19) ◽  
pp. 2463-2468 ◽  
Author(s):  
Po-Huang Liang ◽  
Amnon Kohen ◽  
Timor Baasov ◽  
Karen S. Anderson
Keyword(s):  
Steady State ◽  
Kinetic Analysis ◽  
Catalytic Mechanism ◽  
Steady State Kinetic ◽  
State Kinetic

Influenza virus sialidase: effect of calcium on steady-state kinetic parameters

1991 ◽  
Vol 1077 (1) ◽  
pp. 65-71 ◽  
Author(s):  
Andrew K.J. Chong ◽  
Michael S. Pegg ◽  
Mark von Itzstein
Keyword(s):  
Influenza Virus ◽  
Steady State ◽  
Kinetic Parameters ◽  
Steady State Kinetic ◽  
State Kinetic

The catalytic mechanism of gastric H+/K+-ATPase: simulations of pre-steady-state and steady-state kinetic results

1988 ◽  
Vol 942 (2) ◽  
pp. 215-219 ◽  
Author(s):  
Peter Brzezinski ◽  
Bo G. Malmström ◽  
Pia Lorentzon ◽  
Björn Wallmark
Keyword(s):  
Steady State ◽  
Catalytic Mechanism ◽  
Steady State Kinetic ◽  
State Kinetic

scholarly journals Subsite structure of the endo-type chitin deacetylase from a Deuteromycete, Colletotrichum lindemuthianum: an investigation using steady-state kinetic analysis and MS

2003 ◽  
Vol 374 (2) ◽  
pp. 369-380 ◽  
Author(s):  
Omid HEKMAT ◽  
Ken TOKUYASU ◽  
Stephen G. WITHERS
Keyword(s):  
Steady State ◽  
Kinetic Parameters ◽  
Intrinsic Rate ◽  
Degree Of Polymerization ◽  
Colletotrichum Lindemuthianum ◽  
Chitin Deacetylase ◽  
Steady State Kinetic ◽  
Intrinsic Rate Constant ◽  
Hydrolysis Of ◽  
State Kinetic

The endo-type chitin deacetylase (EC 3.5.1.41) from a Deuteromycete, Colletotrichum lindemuthianum (ATCC 56676), catalyses the hydrolysis of the acetamido group of GlcNAc (2-acetamido-2-deoxy-d-glucose) residues in chitin or chito-oligosaccharides with a degree of polymerization (n) equal to or greater than 2. The steady-state kinetic parameters for the initial deacetylation reactions of (GlcNAc)2–6 were determined using a direct, continuous spectrophotometric assay in combination with ESI-MS (electrospray ionization MS) analysis of the products. The dependence of the observed Km and kcat/Km on n suggests the presence of four enzyme subsites (−2, −1, 0 and +1) that interact with GlcNAc residues from the non-reducing end to the reducing end of the substrate. The turnover number (kcat, 7 s−1) is independent of n and represents the intrinsic rate constant (kint) for the hydrolysis of the acetamido group in subsite 0. The subsite affinities for the GlcNAc residues were calculated from the observed kcat/Km values (A−2, −11.0; A−1, −1.5; A0, −7.7; A+1, −12.5 kJ·mol−1). The increments in the subsite affinities due to the recognition of the acetamido groups were calculated [ΔΔG(N-acetyl)=3.3, 0, 4.0 and 0 kJ·mol−1 for subsites −2, −1, 0 and +1 respectively]. The steady-state kinetic parameters for the second deacetylation reaction of (GlcNAc)4 were also determined using (GlcNAcGlcNAcGlcNGlcNAc) as the substrate. The comparison of the experimental and theoretical values (calculated using the subsite affinities) suggests that the mono-deacetylated substrate binds strongly in a non-productive mode occupying all four subsites, thereby inhibiting the second deacetylation reaction.

Effect of monovalent cations on the pre-steady-state kinetic parameters of the plasma protease activated bovine protein C

Biochemistry ◽  
1985 ◽  
Vol 24 (5) ◽  
pp. 1136-1141 ◽  
Author(s):  
Stephen A. Steiner ◽  
Francis J. Castellino
Keyword(s):  
Steady State ◽  
Kinetic Parameters ◽  
Protein C ◽  
Monovalent Cations ◽  
Steady State Kinetic ◽  
State Kinetic
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