Kinetics of protein modification reactions. Plot of fractional enzyme activity versus extent of protein modification in cases where all modifiable groups are essential for enzyme activity

Rakitzis, Emmanuel T.

doi:10.1042/bj2230259

Cited by 11 publications

(1 citation statement)

References 17 publications

(20 reference statements)

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“…Peak fractions containing the nucleophile label were pooled as indicated (A and B). markedly non-linear, a feature that Rakitzis (1984) suggests is consistent with the involvement of many modifiable groups per active site. Fortunately, in the present case, extensive inactivation was associated with thiol-group modification, so that when this process was taken into consideration (see Figs.…”

Section: Discussionmentioning

confidence: 60%

Identification of an essential glutamic acid residue in β-lactamase II from Bacillus cereus

Little¹,

Emanuel²,

Gagnon³

et al. 1986

Biochemical Journal

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Beta-Lactamase II from Bacillus cereus was readily inactivated by incubation at pH 4.75 with a water-soluble carbodiimide plus a suitable nucleophile. In the early stages of the reaction, 1 equivalent of nucleophile was incorporated/equivalent of enzyme, whereas during the later stages a second equivalent of nucleophile was also incorporated. This latter process correlated with the blocking of the enzyme's single thiol group. Enzyme inactivated in the presence of the coloured nucleophile N-(2,4-dinitrophenyl)ethylenediamine was fragmented by pepsin digestion, and coloured peptides were isolated by gel filtration and h.p.l.c. Two major peptides, representing 52% of the incorporated label, were isolated and sequenced. Both peptides contained the incorporated label on glutamic acid-37, and it is concluded that this latter residue represents a catalytically essential carboxylic residue in beta-lactamase II.

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Section: Discussionmentioning

confidence: 60%

Identification of an essential glutamic acid residue in β-lactamase II from Bacillus cereus

Little¹,

Emanuel²,

Gagnon³

et al. 1986

Biochemical Journal

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Effects of chemical modification on enzymatic activities and stabilities

Sadana

Henley

1986

Biotech & Bioengineering

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The influence of chemical modification on the initial specific activity, residual activity, and deactivation kinetics of various enzymes is analyzed using a series mechanism. This straightforward multistate sequential model presented is consistent with the enzyme deactivation data obtained from different fields. The enzymes are placed in five different categories depending on the effect of chemical modification on initial specific activity and residual activity or stability. Wherever possible, structure-function relationships are described for the enzymes in the different categories. The categorization provides one avenue that leads to further physical insights into enzyme deactivation processes and into the enzyme structure itself.

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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

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Kinetics of protein modification reactions. Plot of fractional enzyme activity versus extent of protein modification in cases where all modifiable groups are essential for enzyme activity

Cited by 11 publications

References 17 publications

Identification of an essential glutamic acid residue in β-lactamase II from Bacillus cereus

Identification of an essential glutamic acid residue in β-lactamase II from Bacillus cereus

Effects of chemical modification on enzymatic activities and stabilities

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

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