The kinetics of enzyme-catalyzed reactions with two or more substrates or products☆I. Nomenclature and rate equations

Ww, Cleland

doi:10.1016/0006-3002(63)91800-6

Cited by 775 publications

(289 citation statements)

References 21 publications

Supporting

Mentioning

270

Contrasting

Unclassified

Order By: Relevance

“…All these micro-reactions are reversible. Since two substrate molecules form one product molecule, the investigated reaction is denoted to follow an ordered bi-uni reaction mechanism (Cleland, 1963). This can be written in Cleland's notation as depicted in Figure 2-7C.…”

Section: Derivation Of the Mechanistic Kinetic Modelmentioning

confidence: 99%

See 1 more Smart Citation

Model-based experimental analysis of enzyme kinetics in aqueous–organic biphasic systems

Zavrel

Schmidt

Michalik

et al. 2007

Journal of Biotechnology

View full text Add to dashboard Cite

Section: Derivation Of the Mechanistic Kinetic Modelmentioning

confidence: 99%

“…Reaction mechanism of a bi-uni-reaction according to Cleland (1963) (C). The optimized experimental conditions listed in Table 4-4 were applied.…”

mentioning

confidence: 99%

Model-based experimental analysis of enzyme kinetics in aqueous–organic biphasic systems

Zavrel

Schmidt

Michalik

et al. 2007

Journal of Biotechnology

View full text Add to dashboard Cite

“…Such information includes the K m for the substrates and the inhibition constant (K i ) for each of the products. Moreover, since TK has a ping-pong kinetic mechanism [22] in which substrates can bind to the``wrong'' enzyme form, there is the potential for substrate inhibition as well.…”

Section: Substrate Speci®citymentioning

confidence: 99%

“…142]. Kinetic studies of DHAS from C. boidinii [74] and TK from E. coli [50] have shown that the properties of these enzymes are consistent with this``ping-pong'' mechanism [22]. Most of the kinetic analyses have been focussed on the investigation of the interactions between TK and its substrates [e.g.…”

Section: Catalytic Mechanism Of Tkmentioning

confidence: 99%

Properties and functions of the thiamin diphosphate dependent enzyme transketolase

Schenk

Duggleby

Nixon

1998

The International Journal of Biochemistry & Cell Biology

223

164

View full text Add to dashboard Cite

This review highlights recent research on the properties and functions of the enzyme transketolase, which requires thiamin diphosphate and a divalent metal ion for its activity. The transketolase-catalysed reaction is part of the pentose phosphate pathway, where transketolase appears to control the non-oxidative branch of this pathway, although the overall¯ux of labelled substrates remains controversial. Yeast transketolase is one of several thiamin diphosphate dependent enzymes whose three-dimensional structures have been determined. Together with mutational analysis these structural data have led to detailed understanding of thiamin diphosphate catalysed reactions. In the homodimer transketolase the two catalytic sites, where dihydroxyethyl groups are transferred from ketose donors to aldose acceptors, are formed at the interface between the two subunits, where the thiazole and pyrimidine rings of thiamin diphosphate are bound. Transketolase is ubiquitous and more than 30 full-length sequences are known. The encoded protein sequences contain two motifs of high homology; one common to all thiamin diphosphate-dependent enzymes and the other a unique transketolase motif. All characterised transketolases have similar kinetic and physical properties, but the mammalian enzymes are more selective in substrate utilisation than the nonmammalian representatives. Since products of the transketolase-catalysed reaction serve as precursors for a number of synthetic compounds this enzyme has been exploited for industrial applications. Putative mutant forms of transketolase, once believed to predispose to disease, have not stood up to scrutiny. However, a modi®cation of transketolase is a marker for Alzheimer's disease, and transketolase activity in erythrocytes is a measure of thiamin nutrition. The cornea contains a particularly high transketolase concentration, consistent with the proposal that pentose phosphate pathway activity has a role in the removal of light-generated radicals. #

show abstract

“…Michaelis constants (Km), dissociation constants (KD) and maximal velocity for the oxidation of BOH and the reduction of NAD+ by the BDH were obtained by mathematical analysis following Cleland (1963).…”

Section: Bdh Kinetic Studiesmentioning

confidence: 99%

Prehibernation and hibernation effects on the d-3-hydroxybutyrate dehydrogenase of the heavy and light mitochondria from liver jerboa (Jaculus orientalis) and related metabolism

Mountassif¹,

Kabine²,

Latruffe³

et al. 2007

Biochimie

View full text Add to dashboard Cite

Kebbaj To cite this version:Driss Mountassif, Mostafa Kabine, Norbert Latruffe, M'Hammed Saïd El Kebbaj. Prehibernation and hibernation effects on the D-3-hydroxybutyrate dehydrogenase of the heavy and light mitochondria from liver jerboa (Jaculus orientalis) and related metabolism.. Biochimie, Elsevier, 2007, 89 (8) Abstract:The D-3-hydroxybutyrate dehydrogenase (BDH) (EC 1.1.1.30) from liver jerboa (Jaculus orientalis), a ketone body converting enzyme in mitochondria, in two populations of mitochondria (heavy and light) has been studied in different jerboa states (euthermic, prehibernatingand hibernating). The results reveal: (1) important variations between states in terms of ketones bodies, glucose and lipid levels; (2) significant differences between the BDH of the two mitochondrial populations in term of protein expression and kinetic properties. These results suggest that BDH leads an important conformational change depending on the physiological state of jerboa. This BDH structural change could be the consequence of the lipid composition modifications in inner mitochondrial membrane leading to changes in BDH catalytic properties.

show abstract

The kinetics of enzyme-catalyzed reactions with two or more substrates or products☆I. Nomenclature and rate equations

Cited by 775 publications

References 21 publications

Model-based experimental analysis of enzyme kinetics in aqueous–organic biphasic systems

Model-based experimental analysis of enzyme kinetics in aqueous–organic biphasic systems

Properties and functions of the thiamin diphosphate dependent enzyme transketolase

Prehibernation and hibernation effects on the d-3-hydroxybutyrate dehydrogenase of the heavy and light mitochondria from liver jerboa (Jaculus orientalis) and related metabolism

Contact Info

Product

Resources

About