Kinetics of protein modification reactions

Rakitzis, Emmanuel T.

doi:10.1042/bj2170341

Cited by 63 publications

(42 citation statements)

References 98 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Ref. 28), however, independent experiments confirmed that the inhibition by this class of compounds was reversible (see also below). It therefore seemed likely that PS-A analogues inhibit IleRS via a slow-binding competitive mechanism that is most commonly described by Scheme 1 (29,30).…”

Section: Resultsmentioning

confidence: 94%

Characterization of Isoleucyl-tRNA Synthetase from Staphylococcus aureus

Pope¹,

Moore²,

McVey³

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

Section: Resultsmentioning

confidence: 94%

Characterization of Isoleucyl-tRNA Synthetase from Staphylococcus aureus

Pope¹,

Moore²,

McVey³

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Under our experimental conditions, about two thiol groups per subunit of P. blakesleeanus isocitrate lyase were modified before complete inactivation, being responsible for 40 and 60% of inactivation, respectively. If the loss of enzyme activity is described by a sum of two exponential functions, then the plot of fractional activity versus the extent of modification of the enzyme groups (Rakitzis, 1984) may be concave-upward, as shown by our results (Fig. 6A).…”

Section: Reactivation Of Inactivated P Blakesleeanus Isocitrate Lyasmentioning

confidence: 79%

Specific and Reversible Inactivation of Phycomyces blakesleeanus Isocitrate Lyase by Ascorbate-Iron: Role of Two Redox-Active Cysteines

Rúa

Soler

Busto

et al. 2002

Fungal Genetics and Biology

View full text Add to dashboard Cite

“…As stated elsewhere [37] in contrast to studies of enzyme catalysis, the thermodynamic and kinetic properties of the reaction of modifying agents with proteins can be compared with the corresponding properties of the reaction of the same modifying agent with small molecules containing the same functional groups as those with which they react in the intact protein. To evaluate this, the B3LYP method and the WASA model were used to evaluate the role of protein local residue changes in the modification process.…”

Section: A Comparison Inmentioning

confidence: 99%

Efficient factors in protein modification: ADenosine deaminase esterification by woodward reagent K

Mahnam

Moosavi‐Movahedi

Bahrami

et al. 2008

JICS

View full text Add to dashboard Cite

Chemical modification of Adenosine Deaminase (ADA) with N-ethyl-5-phenyl isoxazoliom-3 -sulfonate (Woodward's reagent K) (WR-K) was studied using experimental and theoretical techniques. Reaction concentration ranges were 0.8-6 mM WR-K at pH 7.8 and 27 °C. It was observed that the maximum number of moles of esterified residues per mol of enzyme ( ) in this concentration ranges is 4. However, esterification of ADA does not affect the activity of ADA, suggesting that the active site residues are not esterified. Similar results were obtained when the active site was blocked with 0.1 mM erythro-9-(2-hydroxy-3-nonyl) adenine (EHNA), followed by esterification, as measured by enol ester formation using absorbance at 340 nm. A theoretical approach was employed to study the modification process using molecular dynamic simulation, MM and QM/MM minimization. A full ASA empirical model and B3LYP method were used to evaluate the relative stability of some species which may arise from the reaction of ADA with WR-K. Theoretical results have shown that five residues (Glu 244, Glu 121, Glu 337, Asp 127, Asp 338) can be possible cases for modification in reaction 1:1 between ADA and WR-K at = 1. Glu 121 was possible initially modified in this process. Besides, it is specified that atomic accessible surface area cannot be an appropriate criterion in determination of primary sites which are modified by WR-K. Ultimately, it is clarified that among effective factors in modification of enzyme surface such as atomic accessible surface, stability of modified segment and local residues changes of ADA, latter factor plays a basic role in this process from kinetics and thermodynamics point of view.

show abstract

Kinetics of protein modification reactions

Cited by 63 publications

References 98 publications

Characterization of Isoleucyl-tRNA Synthetase from Staphylococcus aureus

Characterization of Isoleucyl-tRNA Synthetase from Staphylococcus aureus

Specific and Reversible Inactivation of Phycomyces blakesleeanus Isocitrate Lyase by Ascorbate-Iron: Role of Two Redox-Active Cysteines

Efficient factors in protein modification: ADenosine deaminase esterification by woodward reagent K

Contact Info

Product

Resources

About