Hydroperoxidic inhibitor of horse liver alcohol-dehydrogenase
activity, tightly bound to the enzyme-NAD+ complex,
characteristically degrades the coenzyme

J 1992

Hydroperoxidic inhibitor of horse liver alcohol-dehydrogenase activity, tightly bound to the enzyme-NAD+ complex, characteristically degrades the coenzyme

SKURSKÝ, Ladislav, Miroslav ŘEZÁČ, Allah N KHAN, Lukáš ŽÍDEK, Jaroslav ROČEK et. al.

Základní údaje

Originální název

Hydroperoxidic inhibitor of horse liver alcohol-dehydrogenase activity, tightly bound to the enzyme-NAD+ complex, characteristically degrades the coenzyme

Autoři

SKURSKÝ, Ladislav, Miroslav ŘEZÁČ, Allah N KHAN, Lukáš ŽÍDEK a Jaroslav ROČEK

Vydání

Journal of Enzyme Inhibition, Reading, Harwood Acad. Publ. GmbH, 1992, 8755-5093

Další údaje

Typ výsledku

Článek v odborném periodiku

Utajení

není předmětem státního či obchodního tajemství

Organizační jednotka

Přírodovědecká fakulta

UT WoS

A1992KC50700004

Klíčová slova anglicky

HORSE LIVHORSE LIVER ALCOHOL DEHYDROGENASE; P-METHYLBENZYL HYDROPEROXIDE;TIGHT-BINDING INHIBITIONER ALCOHOL DEHYDROGENASE; P-METHYLBENZYL HYDROPEROXIDE;TIGHT-BINDING INHIBITION

Štítky

P-METHYLBENZYL HYDROPEROXIDE, TIGHT-BINDING INHIBITION, TIGHT-BINDING INHIBITIONER ALCOHOL DEHYDROGENASE

Změněno: 26. 2. 2003 07:45, prof. Mgr. Lukáš Žídek, Ph.D.

Anotace

V originále

The strong inhibition of horse liver alcohol dehydrogenase (HLAD) by p-methylbenzyl hydroperoxide (XyHP)7 is only transient, XyHP behaves also as a pseudo-substrate of the enzyme and in the presence of NAD+, is degraded by HLAD to (as yet unidentified) non-inhibiting products while the NAD+ is converted to a derivative similar to the "NADX", originally observed in an analogous reaction of HLAD with hydrogen peroxide.4 The apparent K(M) for XyHP is approximately 10(4) times smaller than that for H2O2. The catalytic constant k(cat) for HLAD degradation of XyHP is two orders of magnitude less than that for ethanol dehydrogenation. XyHP inhibits both directions of the alcohol-aldehyde interconversion with equal potency. The first step of the inhibition mechanism is a tight binding of XyHP to the binary HLAD-NAD+ complex.

Citovat

SKURSKÝ, Ladislav, Miroslav ŘEZÁČ, Allah N KHAN, Lukáš ŽÍDEK a Jaroslav ROČEK. Hydroperoxidic inhibitor of horse liver alcohol-dehydrogenase activity, tightly bound to the enzyme-NAD+ complex, characteristically degrades the coenzyme. Journal of Enzyme Inhibition. Reading: Harwood Acad. Publ. GmbH, 1992, roč. 6, č. 3, s. 211-222. ISSN 8755-5093.

@article{362174,
   author = {Skurský, Ladislav and Řezáč, Miroslav and Khan, Allah N and Žídek, Lukáš and Roček, Jaroslav},
   article_location = {Reading},
   article_number = {3},
   keywords = {HORSE LIVHORSE LIVER ALCOHOL DEHYDROGENASE; P-METHYLBENZYL HYDROPEROXIDE;TIGHT-BINDING INHIBITIONER ALCOHOL DEHYDROGENASE; P-METHYLBENZYL HYDROPEROXIDE;TIGHT-BINDING INHIBITION},
   issn = {8755-5093},
   journal = {Journal of Enzyme Inhibition},
   title = {Hydroperoxidic inhibitor of horse liver alcohol-dehydrogenase activity, tightly bound to the enzyme-NAD+ complex, characteristically degrades the coenzyme},
   volume = {6},
   year = {1992}
}

TY  - JOUR
ID  - 362174
AU  - Skurský, Ladislav - Řezáč, Miroslav - Khan, Allah N - Žídek, Lukáš - Roček, Jaroslav
PY  - 1992
TI  - Hydroperoxidic inhibitor of horse liver alcohol-dehydrogenase activity, tightly bound to the enzyme-NAD+ complex, characteristically degrades the coenzyme
JF  - Journal of Enzyme Inhibition
VL  - 6
IS  - 3
SP  - 211
EP  - 211
PB  - Harwood Acad. Publ. GmbH
SN  - 87555093
KW  - HORSE LIVHORSE LIVER ALCOHOL DEHYDROGENASE
KW  - P-METHYLBENZYL HYDROPEROXIDE;TIGHT-BINDING INHIBITIONER ALCOHOL DEHYDROGENASE
KW  - P-METHYLBENZYL HYDROPEROXIDE;TIGHT-BINDING INHIBITION
N2  - The strong inhibition of horse liver alcohol dehydrogenase (HLAD) by p-methylbenzyl hydroperoxide (XyHP)7 is only transient, XyHP behaves also as a pseudo-substrate of the enzyme and in the presence of NAD+, is degraded by HLAD to (as yet unidentified) non-inhibiting products while the NAD+ is converted to a derivative similar to the "NADX", originally observed in an analogous reaction of HLAD with hydrogen peroxide.4 The apparent K(M) for XyHP is approximately 10(4) times smaller than that for H2O2. The catalytic constant k(cat) for HLAD degradation of XyHP is two orders of magnitude less than that for ethanol dehydrogenation. XyHP inhibits both directions of the alcohol-aldehyde interconversion with equal potency. The first step of the inhibition mechanism is a tight binding of XyHP to the binary HLAD-NAD+ complex.
ER  -

SKURSKÝ, Ladislav, Miroslav ŘEZÁČ, Allah N KHAN, Lukáš ŽÍDEK a Jaroslav ROČEK. Hydroperoxidic inhibitor of horse liver alcohol-dehydrogenase activity, tightly bound to the enzyme-NAD+ complex, characteristically degrades the coenzyme. \textit{Journal of Enzyme Inhibition}. Reading: Harwood Acad. Publ. GmbH, 1992, roč.~6, č.~3, s.~211-222. ISSN~8755-5093.

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