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Tytuł:
An easy procedure to transform the ratio of two polynomials of first degree into Michaelis-Menten-type equations. Application to the ordered Uni Bi enzyme mechanism.
Autorzy:
Fontes, Rui
Ribeiro, João
Sillero, Antonio
Powiązania:
https://bibliotekanauki.pl/articles/1044439.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
rectangular hyperbolas
enzyme inhibition
enzyme equations
enzyme kinetics
graphical presentations
Opis:
It is not always clear that some equations affected by complicated factors can, actually, be interpreted as a ratio of two polynomials of first degree and so that they can be, in general, represented by rectangular hyperbolas. In this paper we present an easy procedure to rearrange those equations into Michaelis-Menten-type equations and so to make the aspects of these rectangular hyperbolas more clear, particularly for researchers familiar with general biochemistry. As an example, the method is applied to transform the classical rate equation of the Cleland×s Ordered Uni Bi enzyme mechanism.
Źródło:
Acta Biochimica Polonica; 2000, 47, 1; 259-268
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Inhibition and activation of enzymes. The effect of a modifier on the reaction rate and on kinetic parameters.
Autorzy:
Fontes, Rui
Ribeiro, João
Sillero, Antonio
Powiązania:
https://bibliotekanauki.pl/articles/1044438.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
enzyme inhibition
enzyme modifier
rapid equilibrium kinetics
I50
enzyme activation
enzyme kinetics
graphical presentations
Opis:
A combined analysis of enzyme inhibition and activation is presented, based on a rapid equilibrium model assumption in which one molecule of enzyme binds one molecule of substrate (S) and/or one molecule of a modifier X. The modifier acts as activator (essential or non-essential), as inhibitor (total or partial), or has no effect on the reaction rate (v), depending on the values of the equilibrium constants, the rate constants of the limiting velocity steps, and the concentration of substrate ([S]). Different possibilities have been analyzed from an equation written to emphasize that v = Ł([X]) is, in general and at a fixed [S], a hyperbolic function. Formulas for Su (the value of [S], different from zero, at which v is unaffected by the modifier) and vsu (v at that particular [S]) were deduced. In Lineweaver-Burk plots, the straight lines related to different [X] generally cross in a point (P) with coordinates (Su, vsu). In certain cases, point P is located in the first quadrant which implies that X acts as activator, as inhibitor, or has no effect, depending on [S]. Furthermore, we discuss: (1) the apparent Vmax and Km displayed by the enzyme in different situations; (2) the degree of effect (inhibition or activation) observed at different concentrations of substrate and modifier; (3) the concept of Ke, a parameter that depends on the concentration of substrate and helps to evaluate the effect of the modifier: it equals the value of [X] at which the increase or decrease in the reaction rate is half of that achieved at saturating [X]. Equations were deduced for the general case and for particular situations, and used to obtain computer-drawn graphs that are presented and discussed. Formulas for apparent Vmax, Km and Ke have been written in a way making it evident that these parameters can be expressed as pondered means.
Źródło:
Acta Biochimica Polonica; 2000, 47, 1; 233-257
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Theoretical model explaining the relationship between the molecular mass and the activation energy of the enzyme revealed by a large-scale analysis of bioinformatics data
Autorzy:
Pawlowski, Piotr
Zielenkiewicz, Piotr
Powiązania:
https://bibliotekanauki.pl/articles/1039585.pdf
Data publikacji:
2013
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
statistics
catalysis
turnover
enzyme
molecular mass
Opis:
A general dependence of the enzyme catalytic rate on its mass was revealed when a statistical analysis of 17065 records from the EMP database was performed. The estimated activation energy of the catalytic process decreases asymptotically with the enzyme molecular mass increase. The proposed theoretical model postulates the existence of an intermediate complex of the enzyme and the departing product. It allows for the explanation of the discovered mass-energy relationship, as an effect of the global enzyme-product interactions during complex dissociation. Fitted parameters of the model seem to be in agreement with those widely accepted for the van der Waals energy of molecular interactions. Their values also agree with the picture of the hydrogen bonding in the catalytic process and suggest that surface walk can be the favorable way of the product departure.
Źródło:
Acta Biochimica Polonica; 2013, 60, 2; 239-247
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Correlation between butyrylcholinesterase variants and sensitivity to soman toxicity
Autorzy:
Dimov, Dimo
Kanev, Kamen
Dimova, Ivanka
Powiązania:
https://bibliotekanauki.pl/articles/1039756.pdf
Data publikacji:
2012
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
enzyme inhibition/reactivation
soman toxicity
Butyrylcholinesterase variants
Opis:
Butyrylcholinesterase (BChE) is synthesized in the liver and found in high concentrations in blood plasma, liver, heart, pancreas, vascular endothelium, skin, brain white matter, smooth muscle cells and adipocytes. BChE is a non specific enzyme that hydrolyzes different choline esters (succinylcholine, mivacurium) and many other drugs such as aspirin, cocaine and procaine. The enzyme is also considered as a bioscavenger due to its ability to neutralize the toxic effects of organophosphorus compounds (nervous system fs agents) such as soman. BChE displays several polymorphisms that influence its serum activity; therefore they could determine the individual sensitivity to chemical nerve agents. In this study, we investigated the correlation between BChE variants and the degree of enzyme inhibition and reactivation after soman application on blood samples of 726 individuals. The blood samples of individuals expressing abnormal variants, were more sensitive to soman compared to variants of homozygotes and heterozygotes for U-allele. We found significant differences in the degree of enzyme reactivation between different variants (with and without U-presence).
Źródło:
Acta Biochimica Polonica; 2012, 59, 2; 313-316
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Influence of organic solvents on papain kinetics
Autorzy:
Szabelski, Mariusz
Stachowiak, Krystyna
Wiczk, Wiesław
Powiązania:
https://bibliotekanauki.pl/articles/1044084.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
organic solvent
fluorogenic substrate
enzyme activity
papain
Opis:
Papain activity was studied in water-organic solvent mixtures using the fluorogenic substrate Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans. The increase of organic solvent (MeOH, EtOH, iPrOH, TFE, MeCN, (MeO)2Et and DMF) concentration in the mixture caused a substantial decrease the initial rate of papain-catalyzed hydrolysis. Moreover, the number of papain active sites decreased with the increase of DMF and MeOH concentration.
Źródło:
Acta Biochimica Polonica; 2001, 48, 4; 1197-1201
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Inhibition of the helicase activity of HCV NTPase/helicase by 1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide-5-triphosphate (ribavirin-TP).
Autorzy:
Borowski, Peter
Lang, Melanie
Niebuhr, Andreas
Haag, Annemarie
Schmitz, Herbert
Schulze zur Wiesch, Julian
Choe, Joonho
Siwecka, Maria
Kulikowski, Tadeusz
Powiązania:
https://bibliotekanauki.pl/articles/1044103.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
ribavirin-5'-triphosphate
enzyme inhibition
HCV helicase
Opis:
In the presented study the ribavirin-TP - an established inhibitor of the NTPase activity of the superfamily NTPase/helicases II - was investigated as an inhibitor of the unwinding activity of the hepatitis C virus (HCV) NTPase/helicase. The kinetics of the reaction revealed that ribavirin-TP reduces the turnover number of the helicase reaction by a mechanism that does not correspond to that of the inhibition of the NTPase activity. Our results suggest that derivatives of ribavirin-TP with enhanced stability towards hydrolytic attack may be effective inhibitors of the enzyme.
Źródło:
Acta Biochimica Polonica; 2001, 48, 3; 739-744
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Metabolism of bradykinin in aorta of hypertensive rats
Autorzy:
Bujak-Giżycka, Beata
Olszanecki, Rafał
Madej, Józef
Suski, Maciej
Gębska, Anna
Korbut, Ryszard
Powiązania:
https://bibliotekanauki.pl/articles/1039915.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
bradykinin
angiotensin converting enzyme
mass spectrometry
bioactive peptides
Opis:
Alterations in the formation and metabolism of bradykinin (Bk) are hypothesized to play a role in the pathophysiology of hypertension, atherosclerosis and vascular complications of diabetes. However, despite its prominent role in cardiovascular regulation, studies on bradykinin have been limited by various difficulties in accurate measurements of this peptide in biological samples. In this study, using the LC-ESI-MS method we estimated the conversion of exogenous Bk to its main metabolites - Bk-(1-5) and Bk-(1-7) - in endothelial cell culture and in fragments of aorta of normotensive (WKY) and hypertensive rats (SHR). The effects of angiotensin converting enzyme (ACE) and neutral endopeptidase (NEP) inhibitors were more pronounced in SHR: perindoprilat inhibited Bk-(1-5) formation by 49 % and 76 % in WKY and SHR rats, respectively, and tiorphan tended to decrease formation of Bk-(1-5) in both groups of animals. The degradation of bradykinin and generation of both metabolites were significantly higher in the aorta of SHR rats than in WKY controls. Our results show that even in relatively early hypertension (in 4-month old SHR rats) inactivation of Bk by aorta wall is enhanced.
Źródło:
Acta Biochimica Polonica; 2011, 58, 2; 199-202
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Tissue-specific effect of refeeding after short- and long-term caloric restriction on malic enzyme gene expression in rat tissues.
Autorzy:
Stelmanska, Ewa
Korczynska, Justyna
Swierczynski, Julian
Powiązania:
https://bibliotekanauki.pl/articles/1041561.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
white adipose tissue (rat)
caloric restriction
malic enzyme
refeeding
Opis:
Restricting food intake to a level below that consumed voluntarily (85%, 70% and 50% of the ad libitum energy intake for 3 or 30 days) and re-feeding ad libitum for 48 h results in an increase of malic enzyme (ME) gene expression in rat white adipose tissue. The increase of ME gene expression was much more pronounced in rats maintained on restricted diet for 30 days than for 3 days. The changes in ME gene expression resembled the changes in the content of SREBP-1 in white adipose tissue. A similar increase of serum insulin concentration was observed in all groups at different degrees of caloric restriction and refed ad libitum for 48 h. Caloric restriction and refeeding caused on increase of ME activity also in brown adipose tissue (BAT) and liver. However, in liver a significant increase of ME activity was found only in rats maintained on the restricted diet for 30 days. No significant changes after caloric restriction and refeeding were found in heart, skeletal muscle, kidney cortex, and brain. These data indicate that the increase of ME gene expression after caloric restriction/refeeding occurs only in lipogenic tissues. Thus, one can conclude that caloric restriction/refeeding increases the enzymatic capacity for fatty acid biosynthesis.
Źródło:
Acta Biochimica Polonica; 2004, 51, 3; 805-814
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Influence of dipeptidyl peptidase IV on enzymatic properties of adenosine deaminase
Autorzy:
Sharoyan, Svetlana
Antonyan, Alvard
Mardanyan, Sona
Lupidi, Giulio
Cristalli, Gloria
Powiązania:
https://bibliotekanauki.pl/articles/1041210.pdf
Data publikacji:
2006
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein-protein interaction
large and small adenosine deaminases
CD26-dipeptidyl peptidase IV
enzyme-substrate and enzyme-inhibitor interactions
Opis:
The importance of ADA (adenosine deaminase) in the immune system and the role of its interaction with an ADA-binding cell membrane protein dipeptidyl peptidase IV (DPPIV), identical to the activated immune cell antigen, CD26, has attracted the interest of researchers for many years. To investigate the specific properties in the structure - function relationship of the ADA/DPPIV-CD26 complex, its soluble form, identical to large ADA (LADA), was isolated from human blood serum, human pleural fluid and bovine kidney cortex. The kinetic constants (Km and Vmax) of LADA and of small ADA (SADA), purified from bovine lung and spleen, were compared using adenosine (Ado) and 2'-deoxyadenosine (2'-dAdo) as substrates. The Michaelis constant, Km, evidences a higher affinity of both substrates (in particular of more toxic 2'-dAdo) for LADA and proves the modulation of toxic nucleoside neutralization in the extracellular medium due to complex formation between ADA and DPPIV-CD26. The values of Vmax are significantly higher for SADA, but the efficiency, Vmax /Km, in LADA-catalyzed 2'-dAdo deamination is higher than that in Ado deamination. The interaction of all enzyme preparations with derivatives of adenosine and erythro-9-(2-hydroxy-3-nonyl)adenine (EHNA) was studied. 1-DeazaEHNA and 3-deazaEHNA demonstrate stronger inhibiting activity towards LADA, the DPPIV-CD26-bound form of ADA. The observed differences between the properties of the two ADA isoforms may be considered as a consequence of SADA binding with DPPIV-CD26. Both SADA and LADA indicated a similar pH-profile of adenosine deamination reaction with the optimum at pHs 6.5 - 7.5, while the pH-profile of dipeptidyl peptidase activity of the ADA/DPPIV-CD26 complex appeared in a more alkaline region.
Źródło:
Acta Biochimica Polonica; 2006, 53, 3; 539-546
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Cloning, expression and characterization of thermostable YdaP from Bacillus licheniformis 9A
Autorzy:
Wani Lako, Joseph
Yengkopiong, Jada
Stafford, William
Tuffin, Marla
Cowan, Don
Powiązania:
https://bibliotekanauki.pl/articles/1038524.pdf
Data publikacji:
2018
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Bacillus licheniformis
pyruvate oxidase
YdaP
thiamine diphosphate enzyme
Opis:
The Bacillus licheniformis ydaP gene encodes for a pyruvate oxidase that catalyses the oxidative decarboxylation of pyruvate to acetate and CO2. The YdaP form of this enzyme was purified about 48.6-folds to homogeneity in three steps. The enzyme was recovered in a soluble form and demonstrated significant activity on pyruvate using 2, 6-dichlorophenolindophenol (DCPIP) as an artificial electron acceptor. HPLC analysis of the YdaP-enzyme catalysed conversion of pyruvate showed acetate as the sole product, confirming the putative identity of pyruvate oxidase. Analysis of the substrate specificity showed that the YdaP enzyme demonstrated preference for short chain oxo acids; however, it was activated by 1% Triton X-100. The YdaP substrate-binding pocket from the YdaP protein differed substantially from the equivalent site in all of the so far characterized pyruvate oxidases, suggesting that the B. licheniformis YdaP might accept different substrates. This could allow more accessibility of large substrates into the active site of this enzyme. The thermostability and pH activity of the YdaP enzyme were determined, with optimums at 50ºC and pH 5.8, respectively. The amino acid residues forming the catalytic cavity were identified as Gln460 to Ala480.
Źródło:
Acta Biochimica Polonica; 2018, 65, 1; 59-66
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Influence of Me2SO and incubation time on papain activity studied using fluorogenic substrates.
Autorzy:
Szabelski, Mariusz
Stachowiak, Krystyna
Wiczk, Wiesław
Powiązania:
https://bibliotekanauki.pl/articles/1044042.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
fluorogenic substrate
enzyme activity
papain
Me2SO
Opis:
Papain activity in a buffer containing Me2SO was studied using fluorogenic substrates. It was found that the number of active sites of papain decreases with increasing Me2SO concentration whereas the incubation time, in a buffer containing 3% Me2SO does not affect the number of active sites. However, an increase of papain incubation time in the buffer with 3% Me2SO decreased the initial rate of hydrolysis of Z-Phe-Arg-Amc as well as Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans. Moreover, an increase of Me2SO concentration in working buffer decreased the initial rate of papain-catalysed hydrolysis of both substrates. A rapid decrease of the initial rate (by up to 30%) was observed between 1 and 2% Me2SO. Application of the Michaelis-Menten equation revealed that at the higher Me2SO concentrations the apparent values of kcat/Km decreased as a result of Km increase and kcat decrease. However, Me2SO changed the substrate binding process more effectively (Km) than the rate of catalysis kcat..
Źródło:
Acta Biochimica Polonica; 2001, 48, 4; 995-1002
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
ATP-binding domain of NTPase/helicase as a target for hepatitis C antiviral therapy.
Autorzy:
Borowski, Peter
Mueller, Oliver
Niebuhr, Andreas
Kalitzky, Matthias
Hwang, Lih-Hwa
Schmitz, Herbert
Siwecka, Maria
Kulikowski, Tadeusz
Powiązania:
https://bibliotekanauki.pl/articles/1044428.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
ribavirin-5'-triphosphate
enzyme inhibition
HCV NTPase/helicase
Opis:
To enhance the inhibitory potential of 1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide (ribavirin) vs hepatitis C virus (HCV) NTPase/helicase, ribavirin-5'-triphosphate (ribavirin-TP) was synthesized and investigated. Ribavirin-TP was prepared with the use of modified Yoshikawa-Ludwig-Mishra-Broom procedure (cf. Mishra & Broom, 1991, J. Chem. Soc., Chem. Commun, 1276-1277) involving phosphorylation of unprotected nucleoside. Kinetic analysis revealed enhanced inhibitory potential of ribavirin-TP (IC50=40 μM) as compared to ribavirin (IC50 > 500 μM). Analysis of the inhibition type by means of graphical methods showed a competitive type of inhibition with respect to ATP. In view of the relatively low specificity towards nucleoside-5'-triphosphates (NTP) of the viral NTPase/helicases, it could not be ruled out that the investigated enzyme hydrolyzed the ribavirin-TP to less potent products. Investigations on non- hydrolysable analogs of ribavirin-TP or ribavirin-5'-diphosphate (ribavirin-DP) are currently under way.
Źródło:
Acta Biochimica Polonica; 2000, 47, 1; 173-180
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Ability of Lactobacillus plantarum LS/07 to modify intestinal enzymes activity in chronic diseases prevention
Autorzy:
Hijová, Emília
Kuzma, Jozef
Strojný, Ladislav
Bomba, Alojz
Bertková, Izabela
Chmelárová, Anna
Hertelyová, Zdena
Benetinová, Veronika
Štofilová, Jana
Ambro, Ľuboš
Powiązania:
https://bibliotekanauki.pl/articles/1038694.pdf
Data publikacji:
2017
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Sprague-Dawley rats
bacterial enzyme
cancer
atherosclerosis
dysbiosis
Opis:
The ability of probiotic strain Lactobacillus plantarum LS/07 to modify the activity of intestinal bacterial enzymes - β-glucuronidase (β-GLUCUR), β-galactosidase (β-GAL), and β-glucosidase (β-GLU) in prevention of chronic diseases - cancer, atherosclerosis and dysbiosis was investigated. The male Sprague-Dawley rats were randomly divided into 12 experimental groups: controls groups - C (control), AT (atherosclerotic), CC (carcinogenic), dysbiotic groups - each group in combination with antibiotics (ATB), probiotics groups - in combinatioan with probiotic (PRO) alone, and each group with combination of antibiotic and probiotic (ATB+PRO). In the control group the β-glucuronidase activity did not change throughout the experiment. High fat diet in atherosclerotic group significantly increased the activity of β-glucuronidase (P<0.001) and β-glucosidase (P<0.01). Azoxymethane application in carcinogenic group significantly increased β-glucuronidase (P<0.01), but reduced β-glucosidase (P<0.01) activity. Daily application of probiotics alone and in combination with antibiotic increased β-galactosidase, of β-glucosidase, and decreased β-glucuronidase activity. In control antibiotic group we observed significant increase in β-glucuronidase (P<0.05) and decreased β-glucosidase (P<0.01) activity which can be caused by the change of microflora in favor of coliform bacteria. These findings indicate the positive effects of probiotic Lactobacillus plantarum LS/07 and suggest its use in disease prevention in human medicine and some animal species.
Źródło:
Acta Biochimica Polonica; 2017, 64, 1; 113-116
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Farnesyl diphosphate synthase; regulation of product specificity.
Autorzy:
Szkopińska, Anna
Płochocka, Danuta
Powiązania:
https://bibliotekanauki.pl/articles/1041460.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
modulation of enzyme activity
dimer structure
gene family
FPP synthase
Opis:
Farnesyl diphosphate synthase (FPPS) is a key enzyme in isoprenoid biosynthesis which supplies sesquiterpene precursors for several classes of essential metabolites including sterols, dolichols, ubiquinones and carotenoids as well as substrates for farnesylation and geranylgeranylation of proteins. It catalyzes the sequential head-to-tail condensation of two molecules of isopentenyl diphosphate with dimethylallyl diphosphate. The enzyme is a homodimer of subunits, typically having two aspartate-rich motifs with two sets of substrate binding sites for an allylic diphosphate and isopentenyl diphosphate per homodimer. The synthase amino-acid residues at the 4th and 5th positions before the first aspartate rich motif mainly determine product specificity. Hypothetically, type I (eukaryotic) and type II (eubacterial) FPPSs evolved from archeal geranylgeranyl diphosphate synthase by substitutions in the chain length determination region. FPPS belongs to enzymes encoded by gene families. In plants this offers the possibility of differential regulation in response to environmental changes or to herbivore or pathogen attack.
Źródło:
Acta Biochimica Polonica; 2005, 52, 1; 45-55
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Kinetic analysis of the transient phase and steady state of open multicyclic enzyme cascades
Autorzy:
Varón, Ramón
Havsteen, Bent
Valero, Edelmira
Molina-Alarcón, Milagros
García-Cánovas, Francisco
García-Moreno, Manuela
Powiązania:
https://bibliotekanauki.pl/articles/1041315.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
steady state
fractional modification
transient phase
enzyme kinetics
multicyclic cascades
Opis:
This paper presents a kinetic analysis of the whole reaction course, i.e. of both the transient phase and the steady state, of open multicyclic enzyme cascade systems. Equations for fractional modifications are obtained which are valid for the whole reaction course. The steady state expressions for the fractional modifications were derived from the latter equations since they are not restricted to the condition of rapid equilibrium. Finally, the validity of our results is discussed and tested by numerical integration. Apart from the intrinsic value of knowing the kinetic behaviour of any of the species involved in any open multicyclic enzyme cascade, the kinetic analysis presented here can be the basis of future contributions concerning open multicyclic enzyme cascades which require the knowledge of their time course equations (e.g. evaluation of the time needed to reach the steady state, suggestion of kinetic data analysis, etc.), analogous to those already carried out for open bicyclic cascades.
Źródło:
Acta Biochimica Polonica; 2005, 52, 4; 765-780
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
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