Unusual steady-state kinetic properties of a chilopod enzyme

l(+)lactate dehydrogenase purified from Scolopendra cingulata

Massimo Dell'Agata, Gianna Pannunzio, Margherita Annicchiarico, Annamaria Coscarella, Alessandro Ferracin

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

1. 1. Lactate dehydrogenase was purified to homogeneity from the chilopod Scolopendra cingulata. 2. 2. The enzyme has the usual molecular weight of approximately 150,000 and exists as a tetramer. It is l(+)lactate specific and some lines of evidence ascribe the molecule to the A-class (muscle-type of vertebrates). 3. 3. Surprisingly it displays Kcat values for both substrates pyruvate and lactate which are about two orders of magnitude lower than those known for other lactate dehydrogenases. 4. 4. Additionally, both Km for lactate and Kcat/Km for pyruvate are independent from assay temperature. 5. 5. The most striking feature of this enzyme, however, is its stability, as it still retains activity either after incubation at 90°C or in the presence of urea concentrations as high as 7.5 M.

Original languageEnglish
Pages (from-to)439-444
Number of pages6
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Volume96
Issue number3
DOIs
Publication statusPublished - 1990

Fingerprint

L-Lactate Dehydrogenase
Lactic Acid
Pyruvic Acid
Kinetics
Lactate Dehydrogenases
Enzymes
Muscle
Vertebrates
Urea
Assays
Molecular Weight
Molecular weight
Muscles
Molecules
Temperature
Substrates
scolopendra

ASJC Scopus subject areas

  • Biochemistry
  • Physiology

Cite this

Unusual steady-state kinetic properties of a chilopod enzyme : l(+)lactate dehydrogenase purified from Scolopendra cingulata. / Dell'Agata, Massimo; Pannunzio, Gianna; Annicchiarico, Margherita; Coscarella, Annamaria; Ferracin, Alessandro.

In: Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, Vol. 96, No. 3, 1990, p. 439-444.

Research output: Contribution to journalArticle

@article{5977e0a5914a43af9f6a1c4a1a190db3,
title = "Unusual steady-state kinetic properties of a chilopod enzyme: l(+)lactate dehydrogenase purified from Scolopendra cingulata",
abstract = "1. 1. Lactate dehydrogenase was purified to homogeneity from the chilopod Scolopendra cingulata. 2. 2. The enzyme has the usual molecular weight of approximately 150,000 and exists as a tetramer. It is l(+)lactate specific and some lines of evidence ascribe the molecule to the A-class (muscle-type of vertebrates). 3. 3. Surprisingly it displays Kcat values for both substrates pyruvate and lactate which are about two orders of magnitude lower than those known for other lactate dehydrogenases. 4. 4. Additionally, both Km for lactate and Kcat/Km for pyruvate are independent from assay temperature. 5. 5. The most striking feature of this enzyme, however, is its stability, as it still retains activity either after incubation at 90°C or in the presence of urea concentrations as high as 7.5 M.",
author = "Massimo Dell'Agata and Gianna Pannunzio and Margherita Annicchiarico and Annamaria Coscarella and Alessandro Ferracin",
year = "1990",
doi = "10.1016/0305-0491(90)90036-S",
language = "English",
volume = "96",
pages = "439--444",
journal = "Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology",
issn = "1096-4959",
publisher = "Elsevier Inc.",
number = "3",

}

TY - JOUR

T1 - Unusual steady-state kinetic properties of a chilopod enzyme

T2 - l(+)lactate dehydrogenase purified from Scolopendra cingulata

AU - Dell'Agata, Massimo

AU - Pannunzio, Gianna

AU - Annicchiarico, Margherita

AU - Coscarella, Annamaria

AU - Ferracin, Alessandro

PY - 1990

Y1 - 1990

N2 - 1. 1. Lactate dehydrogenase was purified to homogeneity from the chilopod Scolopendra cingulata. 2. 2. The enzyme has the usual molecular weight of approximately 150,000 and exists as a tetramer. It is l(+)lactate specific and some lines of evidence ascribe the molecule to the A-class (muscle-type of vertebrates). 3. 3. Surprisingly it displays Kcat values for both substrates pyruvate and lactate which are about two orders of magnitude lower than those known for other lactate dehydrogenases. 4. 4. Additionally, both Km for lactate and Kcat/Km for pyruvate are independent from assay temperature. 5. 5. The most striking feature of this enzyme, however, is its stability, as it still retains activity either after incubation at 90°C or in the presence of urea concentrations as high as 7.5 M.

AB - 1. 1. Lactate dehydrogenase was purified to homogeneity from the chilopod Scolopendra cingulata. 2. 2. The enzyme has the usual molecular weight of approximately 150,000 and exists as a tetramer. It is l(+)lactate specific and some lines of evidence ascribe the molecule to the A-class (muscle-type of vertebrates). 3. 3. Surprisingly it displays Kcat values for both substrates pyruvate and lactate which are about two orders of magnitude lower than those known for other lactate dehydrogenases. 4. 4. Additionally, both Km for lactate and Kcat/Km for pyruvate are independent from assay temperature. 5. 5. The most striking feature of this enzyme, however, is its stability, as it still retains activity either after incubation at 90°C or in the presence of urea concentrations as high as 7.5 M.

UR - http://www.scopus.com/inward/record.url?scp=0025324924&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025324924&partnerID=8YFLogxK

U2 - 10.1016/0305-0491(90)90036-S

DO - 10.1016/0305-0491(90)90036-S

M3 - Article

VL - 96

SP - 439

EP - 444

JO - Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology

JF - Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology

SN - 1096-4959

IS - 3

ER -