KM

(redirected from Michaelis-Menten constant)
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AcronymDefinition
KMKilometer
KMComoros (ISO country code, top level domain)
KMKnowledge Management
KMKarl Marx (philospher)
KMKonica Minolta (camera)
KMKaltmiete (German: rent without utilities)
KMAir Malta (IATA airline code)
KMKiss Me
KMK-Mart
KMKrav Maga (Israeli martial art)
KMKyocera Mita (various locations)
KMKriegsmarine (WWII German Navy)
KMKey Management
KMKnights of Malta (religious order)
KMKoninklijke Marine (Royal Navy)
KMKilling Machine (short movie)
KMMichaelis-Menten Constant (molececular cellular biology)
KMKitchen Manager (restaurants)
KMKarl Malone (NBA Player)
KMKnight of Malta
KMKarabin Maszynowy (Polish: Machine Gun)
KMKevin Mitnick (former hacker)
KMKnightmare (gaming clan)
KMKrause-Mishler (numismatic catalogue)
KMKashimashi (anime)
KMKabataang Makabayan (Nationalist Youth, Philippines)
KMKick Me
KMKent Messenger (newspaper, England)
KMKashmiri Migrant (India)
KMKeith Mcleod (NBA Player)
KMKinematic Mount
KMKeyboard Mania (keyboard simulation game)
KMKilomega (archaic; now Giga-)
KMKiller Mongoose (UK gaming clan)
KMKingd Mickey (video game character, Kingdom Hearts)
KMKirk-Mayer, Inc
KMUnited Kingdom to Mediterranean (routing designation; US Navy)
References in periodicals archive ?
In this research, Michaelis-Menten kinetic (Michaelis-Menten constant (Km) and maximum uptake rate (Imax)) provides a useful tool for the identification of plant nutrient uptake efficiency and selection of plants.
The Michaelis-Menten constant is important to characterize the enzyme electrode due to the character of the aforementioned constant (KM).
Theoretical maximal reaction velocities (Vmax) and Michaelis-Menten constant (Km) were calculated against CMC using Lineweaver-Bulk plot (Table 1).
where V, [V.sub.max], [K.sub.m], and [S] are reaction rate, maximum reaction rate, Michaelis-Menten constant, and substrate concentration, respectively.
where Ki refers to inhibition constant; IC50 refers to concentration of fluorinated bile acid that causes a 50% decrease in [sup.3]H labeled substrate uptake; [S] refers to concentration of [sup.3]H labeled substrate; Km refers to Michaelis-Menten constant of [sup.3]H labeled substrate
The apparent Michaelis-Menten constant ([K.sub.m]), an indicator of enzyme-substrate reaction kinetics, can be used to evaluate the biological activity of the immobilized enzyme, and this constant can be calculated from the Lineweaver-Burk equation, given below:
In [11], the presented model was derived from the work of diffusion in a punctual iontophoretic source where the lineal term of absorption is replaced by a nonlinear expression that describes a Michaelis-Menten kinetic given by a constant [V.sub.m], the Michaelis-Menten constant [K.sub.m].
where [I.sub.peak,c] is the peak current at the substrate concentration C, [I.sub.peak,max] is the peak current at saturating substrate conditions, and [K.sup.app.sub.m,el], is a constant with the same meaning as the Michaelis-Menten constant [K.sup.app.sub.m,el].
We use Michaelis-Menten kinetics in order to have a mixed-order model for the pharmacokinetics, so this equation results in the term [[??].sub.3] = -c[x.sub.3]/([K.sub.B] + [x.sub.3]), where the parameter [K.sub.B] is the Michaelis-Menten constant of the inhibitor;
Abbreviations: CEC, 3-cyano-7-ethoxycoumarin; CYP, cytochrome P450; DMSO, dimethylsulfoxide; [K.sub.m], Michaelis-Menten constant; Vmax, maximum velocity; [IC.sub.50], the half maximal (50%) inhibitory concentration; [K.sub.i], the inhibitor concentration required for a half-maximal inhibition; NADPH, nicotinamide adenine dinucleotide phosphate.
In order to determine the maximum velocity (Vmax) and Michaelis-Menten constant (Km) of the glutaminase enzyme we plotted Lineweaver-Burk graph (Fig.
Table 2 shows the Michaelis-Menten constant (Km,app) and maximal velocity (Vmax,app) of the enzyme in hydrolyzing three different substrates; ATC, BTC and PTC.