Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase

Marysol Alvear, Ana María Jabalquinto, Jaime Eyzaguirre, Emilio Cardemil

Resultado de la investigación: Article

36 Citas (Scopus)

Resumen

Mevalonate-5-pyrophosphate decarboxylase [ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33] has been purified 5800 times from chicken liver and obtained in a stable and highly purified form. The protein is a dimer of molecular weight 85 400 ± 1941, and its subunits were not resolved by gel electrophoresis in denaturing conditions. The purified enzyme does not require the presence of SH-containing reagents for either activity or stability. The enzyme shows a high specificity for adenosine 5′-triphosphate (ATP) and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 4.0 to 6.5. Inhibitory effects for the enzyme activity were detected by citrate, phthalate, and phosphate. The isoelectric point, as determined by column chromatofocusing, is 4.8. The kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.0141 mM and 0.504 mM have been obtained for mevalonate-5-pyrophosphate and ATP, respectively.

Idioma originalEnglish
Páginas (desde-hasta)4646-4650
Número de páginas5
PublicaciónBiochemistry
Volumen21
N.º19
EstadoPublished - 1982

Huella dactilar

pyrophosphomevalonate decarboxylase
Mevalonic Acid
Carboxy-Lyases
Liver
Adenosine Diphosphate
Purification
Adenosine Triphosphate
Enzymes
Sulfhydryl Reagents
Divalent Cations
Isoelectric Point
Enzyme activity
Electrophoresis
Citric Acid
Dimers
Adenosine
Cations
Chickens
Molecular Weight
Gels

ASJC Scopus subject areas

  • Biochemistry

Citar esto

Alvear, M., Jabalquinto, A. M., Eyzaguirre, J., & Cardemil, E. (1982). Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase. Biochemistry, 21(19), 4646-4650.
Alvear, Marysol ; Jabalquinto, Ana María ; Eyzaguirre, Jaime ; Cardemil, Emilio. / Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase. En: Biochemistry. 1982 ; Vol. 21, N.º 19. pp. 4646-4650.
@article{3d67d51aad2c4731baddd9c5e3ca4b70,
title = "Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase",
abstract = "Mevalonate-5-pyrophosphate decarboxylase [ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33] has been purified 5800 times from chicken liver and obtained in a stable and highly purified form. The protein is a dimer of molecular weight 85 400 ± 1941, and its subunits were not resolved by gel electrophoresis in denaturing conditions. The purified enzyme does not require the presence of SH-containing reagents for either activity or stability. The enzyme shows a high specificity for adenosine 5′-triphosphate (ATP) and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 4.0 to 6.5. Inhibitory effects for the enzyme activity were detected by citrate, phthalate, and phosphate. The isoelectric point, as determined by column chromatofocusing, is 4.8. The kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.0141 mM and 0.504 mM have been obtained for mevalonate-5-pyrophosphate and ATP, respectively.",
author = "Marysol Alvear and Jabalquinto, {Ana Mar{\'i}a} and Jaime Eyzaguirre and Emilio Cardemil",
year = "1982",
language = "English",
volume = "21",
pages = "4646--4650",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "19",

}

Alvear, M, Jabalquinto, AM, Eyzaguirre, J & Cardemil, E 1982, 'Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase', Biochemistry, vol. 21, n.º 19, pp. 4646-4650.

Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase. / Alvear, Marysol; Jabalquinto, Ana María; Eyzaguirre, Jaime; Cardemil, Emilio.

En: Biochemistry, Vol. 21, N.º 19, 1982, p. 4646-4650.

Resultado de la investigación: Article

TY - JOUR

T1 - Purification and characterization of avian liver mevalonate-5-pyrophosphate decarboxylase

AU - Alvear, Marysol

AU - Jabalquinto, Ana María

AU - Eyzaguirre, Jaime

AU - Cardemil, Emilio

PY - 1982

Y1 - 1982

N2 - Mevalonate-5-pyrophosphate decarboxylase [ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33] has been purified 5800 times from chicken liver and obtained in a stable and highly purified form. The protein is a dimer of molecular weight 85 400 ± 1941, and its subunits were not resolved by gel electrophoresis in denaturing conditions. The purified enzyme does not require the presence of SH-containing reagents for either activity or stability. The enzyme shows a high specificity for adenosine 5′-triphosphate (ATP) and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 4.0 to 6.5. Inhibitory effects for the enzyme activity were detected by citrate, phthalate, and phosphate. The isoelectric point, as determined by column chromatofocusing, is 4.8. The kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.0141 mM and 0.504 mM have been obtained for mevalonate-5-pyrophosphate and ATP, respectively.

AB - Mevalonate-5-pyrophosphate decarboxylase [ATP:5-diphosphomevalonate carboxy-lyase (dehydrating), EC 4.1.1.33] has been purified 5800 times from chicken liver and obtained in a stable and highly purified form. The protein is a dimer of molecular weight 85 400 ± 1941, and its subunits were not resolved by gel electrophoresis in denaturing conditions. The purified enzyme does not require the presence of SH-containing reagents for either activity or stability. The enzyme shows a high specificity for adenosine 5′-triphosphate (ATP) and requires for activity a divalent metal cation, Mg2+ being most effective. The optimum pH for the enzyme ranges from 4.0 to 6.5. Inhibitory effects for the enzyme activity were detected by citrate, phthalate, and phosphate. The isoelectric point, as determined by column chromatofocusing, is 4.8. The kinetics are hyperbolic for both substrates, showing a sequential mechanism; true Km values of 0.0141 mM and 0.504 mM have been obtained for mevalonate-5-pyrophosphate and ATP, respectively.

UR - http://www.scopus.com/inward/record.url?scp=0020482349&partnerID=8YFLogxK

M3 - Article

VL - 21

SP - 4646

EP - 4650

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 19

ER -