scholarly journals Assessment of hepatic pyruvate carboxylase activity using hyperpolarized [1‐ 13 C]‐ l ‐lactate

2020 ◽  
Vol 85 (3) ◽  
pp. 1175-1182
Author(s):  
Jun Chen ◽  
Edward P. Hackett ◽  
Zoltan Kovacs ◽  
Craig R. Malloy ◽  
Jae Mo Park
Keyword(s):  
Pyruvate Carboxylase ◽  
Carboxylase Activity

THIAMINE-RESPONSIVE LACTIC ACIDOSIS IN A PATIENT WITH DEFICIENT LOW-KM PYRUVATE CARBOXYLASE ACTIVITY IN LIVER

PEDIATRICS ◽  
1972 ◽  
Vol 50 (5) ◽  
pp. 702-711
Author(s):  
Michèle G. Brunette ◽  
Edgard Delvin ◽  
Bernard Hazel ◽  
Charles R. Scriver
Keyword(s):  
Lactic Acidosis ◽  
Pyruvate Dehydrogenase ◽  
Pyruvate Carboxylase ◽  
Acid Metabolism ◽  
Psychomotor Retardation ◽  
Dietary Control ◽  
Carboxylase Activity ◽  
Cultured Skin ◽  
Carbohydrate Feeding ◽  
Partial Deficiency

The cause of severe intermittent lactic acidosis was investigated in a female infant with profound psychomotor retardation. Hypoglycemia, hyperpyruvic acidemia, and hyperalaninemia were identified in the newborn period. A triad of lactate, pyruvate, and alanine accumulation persisted throughout infancy, and ACTH, anorexia, and high carbohydrate feeding further provoked their accumulation. Careful dietary control or thiamine-HCl supplementation (5 to 20 mg/day) ameliorated the metabolic abnormality. Pyruvate dehydrogenase activity (which is thiamine-dependent) was normal in leukocytes and cultured skin fibroblasts. Hepatic pyruvate carboxylase activity (which is biotin-dependent) was found to comprise more than one component. There was a partial deficiency of total hepatic pyruvate carboxylase activity in the patient. The loss of activity was confined to the low-Km component of the enzyme which serves pvruvate metabolism in the physiological range. A defect in glucogenesis causing hypoglycemia, pyruvate accumulation with lactic acidosis, and aberrant amino acid metabolism can be attributed to the abnormality of pyruvate carboxylase. The response to thiamine in our patients may reflect activation of a normal "shunt" mechanism for pyruvate disposal via pyruvate dehydrogenase.

Role of salicylic acid in regulation of cadmium toxicity in wheat ( Triticum aestivum L.)

2009 ◽  
Vol 57 (3) ◽  
pp. 321-333 ◽  
Author(s):  
H. Moussa ◽  
S. EL-Gamal
Keyword(s):  
Pyruvate Carboxylase ◽  
Cadmium Toxicity ◽  
Triticum Aestivum L ◽  
Carboxylase Activity ◽  
Bisphosphate Carboxylase ◽  
Cd Accumulation ◽  
Phosphoenol Pyruvate ◽  
Relative Water ◽  
Aba Content

Treatment with CdCl 2 (0, 100, 400 and 1000 μM) resulted in the inhibition of root dry biomass and root elongation and to increased Cd accumulation in the roots. These treatments also decreased the relative water content, chlorophyll content, 14 CO fixation, phosphoenol pyruvate carboxylase and ribulose-1,5-bisphosphate carboxylase activity and abscisic acid (ABA) content, while increasing the malondialdehyde, hydrogen peroxide and free proline contents and causing changes in the chloroplast and root ultrastructure. Pretreatment of seeds with SA (500 μM) for 20 h resulted in the amelioration of these effects.

Pyruvate carboxylase activity is not abnormal in fibroblasts of patients with Friedreich's ataxia

1984 ◽  
Vol 16 (2) ◽  
pp. 262-262 ◽  
Author(s):  
U. J. Dijkstra ◽  
J. M. F. Trijbels ◽  
W. Ruitenbeek ◽  
J. A. J. M. Bakkeren ◽  
A. J. M. Janssen ◽  
...  
Keyword(s):  
Pyruvate Carboxylase ◽  
Friedreich’S Ataxia ◽  
Friedreich's Ataxia ◽  
Carboxylase Activity

scholarly journals Calcitonin increases pyruvate carboxylase activity in hepatic mitochondria of rats.

1981 ◽  
Vol 28 (6) ◽  
pp. 709-714 ◽  
Author(s):  
MASAYOSHI YAMAGUCHI ◽  
MASATSUGU KURA
Keyword(s):  
Pyruvate Carboxylase ◽  
Carboxylase Activity

scholarly journals In vivo phospho enol pyruvate carboxylase activity is controlled by CO 2 and O 2 mole fractions and represents a major flux at high photorespiration rates

2018 ◽  
Vol 221 (4) ◽  
pp. 1843-1852 ◽  
Author(s):  
Cyril Abadie ◽  
Guillaume Tcherkez
Keyword(s):  
Pyruvate Carboxylase ◽  
Carboxylase Activity

Pyruvate carboxylase activity in subacute necrotizing encephalopathy (Leigh's disease)

Neurology ◽  
1984 ◽  
Vol 34 (4) ◽  
pp. 515-515 ◽  
Author(s):  
J. Sander ◽  
S. Packman ◽  
B. O. Berg ◽  
H. T. Hutchison ◽  
N. Caswell
Keyword(s):  
Pyruvate Carboxylase ◽  
Carboxylase Activity ◽  
Leigh's Disease

scholarly journals Effect of Pyruvate Carboxylase Overexpression on the Physiology of Corynebacterium glutamicum

2002 ◽  
Vol 68 (11) ◽  
pp. 5422-5428 ◽  
Author(s):  
Mattheos A. G. Koffas ◽  
Gyoo Yeol Jung ◽  
Juan C. Aon ◽  
Gregory Stephanopoulos
Keyword(s):  
Corynebacterium Glutamicum ◽  
Pyruvate Carboxylase ◽  
Carbon Sources ◽  
Acid Synthesis ◽  
Aspartate Kinase ◽  
Growth Enhancement ◽  
Lysine Production ◽  
Carboxylase Activity ◽  
Amino Acid Synthesis ◽  
Permeabilized Cells

ABSTRACT Pyruvate carboxylase was recently sequenced in Corynebacterium glutamicum and shown to play an important role of anaplerosis in the central carbon metabolism and amino acid synthesis of these bacteria. In this study we investigate the effect of the overexpression of the gene for pyruvate carboxylase (pyc) on the physiology of C. glutamicum ATCC 21253 and ATCC 21799 grown on defined media with two different carbon sources, glucose and lactate. In general, the physiological effects of pyc overexpression in Corynebacteria depend on the genetic background of the particular strain studied and are determined to a large extent by the interplay between pyruvate carboxylase and aspartate kinase activities. If the pyruvate carboxylase activity is not properly matched by the aspartate kinase activity, pyc overexpression results in growth enhancement instead of greater lysine production, despite its central role in anaplerosis and aspartic acid biosynthesis. Aspartate kinase regulation by lysine and threonine, pyruvate carboxylase inhibition by aspartate (shown in this study using permeabilized cells), as well as well-established activation of pyruvate carboxylase by lactate and acetyl coenzyme A are the key factors in determining the effect of pyc overexpression on Corynebacteria physiology.

A method for the determination of pyruvate carboxylase activity during the glutamic acid fermentation with Corynebacterium glutamicum

1999 ◽  
Vol 39 (1) ◽  
pp. 91-96 ◽  
Author(s):  
Davin Uy ◽  
Stéphane Delaunay ◽  
Jean-Marc Engasser ◽  
Jean-Louis Goergen
Keyword(s):  
Glutamic Acid ◽  
Corynebacterium Glutamicum ◽  
Pyruvate Carboxylase ◽  
Acid Fermentation ◽  
Carboxylase Activity
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