2 edition of Characterization of mutations in the E1[alpha] subunit of the pyruvate dehydrogenase complex. found in the catalog.
Characterization of mutations in the E1[alpha] subunit of the pyruvate dehydrogenase complex.
Kathy M. Chun
Written in English
|The Physical Object|
|Number of Pages||221|
The most common cause are mutations in thePDHA1 gene (Xp), which encodes the E1-alpha subunit. Mutations in the genes for the other subunits have been described, but are far less frequent: E1-beta and E2 subunits (PDHB, DLAT); E3 binding protein (PDHX gene); and E3 and PDH phosphatase (DLD andPDP1). This IHC data was generated using the same phospho anti-Pyruvate Dehydrogenase E1-alpha antibody clone, EPR, in a different buffer formulation (cat# ab). Immunohistochemical analysis of paraffin-embedded Human colon tissue labeling Pyruvate dehydrogenase E1-alpha subunit with ab at 1/50 dilution.
A mutation in the gene encoding the E1 subunit of the pyruvate dehydrogenase complex was shown to be sufficient to rescue the lack of DXS but not DXR in vivo, suggesting that the mutant enzyme likely allows the synthesis of DXP or an alternative substrate for DXR. was selected for further characterization. A mutation in the aceE gene Cited by: Pyruvate dehydrogenase (lipoamide) beta, also known as pyruvate dehydrogenase E1 component subunit beta, mitochondrial or PDHE1-B is an enzyme that in humans is encoded by the PDHB gene. The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO 2, and provides the Aliases: PDHB, PDHBD, PDHE1-B, PHE1B, Pyruvate .
Pyruvate dehydrogenase deficiency is a major cause of primary lactic acidosis and neurological dysfunction in infancy and early childhood. Most cases are caused by mutations in the X-linked gene for the E1alpha subunit of the complex. Mutations in DLAT, . In a male patient with lactic acidosis and decreased pyruvate dehydrogenase E1 activity (PDHAD; ), Endo et al. () identified a 4-bp deletion in the PDHA1 cDNA ().In a female patient with PDH deficiency and decreased levels of the E1-alpha subunit, Dahl et al. () identified a 7-bp deletion in the PDHA1 gene ().The authors noted that the severity of the.
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Isolation of a full-length complementary DNA coding for human E1 alpha subunit of the pyruvate dehydrogenase complex. J Biol Chem. Feb 5; (4)– Endo H, Hasegawa K, Narisawa K, Tada K, Kagawa Y, Ohta S.
Defective gene in lactic acidosis: abnormal pyruvate dehydrogenase E1 alpha-subunit caused by a frame shift. Am J Hum by: The human pyruvate dehydrogenase complex catalyses the oxidative decarboxylation of pyruvate to acetyl-CoA.
Defects in several of the seven subunits have been reported, but the majority of mutations affect the E1 component and especially the E1α subunit. However, the clinical presentation of patients with pyruvate dehydrogenase E1α deficiency is extremely by: Mycoplasma synoviae (MS) is an important pathogen, causing enormous economic losses to the poultry industry worldwide every year.
Therefore, the studies on MS will lay the foundation for diagnosis, prevention and treatment of MS infection. In this study, primers designed based on the sequences of pyruvate dehydrogenase complex (PDC) E1 alpha and beta subunit genes (pdhA Author: Shijun Bao, Xiaoqin Ding, Shengqing Yu, Chan Ding.
Mutations in the X-linked pyruvate dehydrogenase (E1) alpha subunit gene (PDHA1) in patients with a pyruvate dehydrogenase complex deficiency.
Lissens W(1), De Meirleir L, Seneca S, Liebaers I, Brown GK, Brown RM, Ito M, Naito E, Kuroda Y, Kerr DS, Wexler ID, Patel MS, Robinson BH, Seyda by: Cite this article.
Wexler, I., Hemalatha, S., Liu, T. et al. A Mutation in the E 1 α Subunit of Pyruvate Dehydrogenase Associated with Variable Expression of Pyruvate Dehydrogenase Complex Cited by: The human pyruvate dehydrogenase complex catalyses the oxidative decarboxylation of pyruvate to acetyl-CoA.
Defects in several of the seven subunits have been reported, but the majority of mutations affect the E1 component and especially the E1 alpha by: Pyruvate dehydrogenase (E1), an alpha 2 beta 2 tetramer, is the first component of the pyruvate dehydrogenase complex which catalyzes a two-step oxidative decarboxylation of pyruvic acid.
Pyruvate dehydrogenase E1-alpha deficiency (PDHAD) results in lactic acidosis and hyperpyruvatemia. Two patients with PDHAD, a man with a mutation, and a girl with a mutation in Author: Takanobu Yoshida, Jun Kido, Hiroshi Mitsubuchi, Shirou Matsumoto, Fumio Endo, Kimitoshi Nakamura.
A cDNA clone ( base pairs) comprising the entire coding region of the precursor form of the alpha subunit of pyruvate dehydrogenase (E1 alpha) has been isolated from a human liver cDNA library. Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase.
Two individuals with pyruvate dehydrogenase (PDH) deﬁciency due to missense mutations in the gene for the E1 α subunit (PDHA1) presented during childhood with dystonia. The ﬁrst patient, a male, presented at age 4 years with dystonia affecting the lower limbs, which responded to treatment with combined carbidopa and by: The human pyruvate dehydrogenase complex.
Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA. J Biol Chem. May 25; (15)– De Meirleir L, MacKay N, Lam Hon Wah AM, Robinson BH. Isolation of a full-length complementary DNA coding for human E1 alpha subunit of the pyruvate.
Pyruvate dehydrogenase (E1) is a tetramer of 2 alpha and 2 beta subunits. Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X.
An Arabidopsis cDNA encoding the dihydrolipoamide S -acetyltransferase subunit of the plastid pyruvate dehydrogenase complex (E2) was isolated from a λPRL2 library. The cDNA is bp in length, with a continuous open reading frame of bp encoding a protein of amino acids with a calculated molecular mass of 50, D.
Southern analysis suggests that a single gene encodes Cited by: 1. Introduction. Mammalian pyruvate dehydrogenase complex (PDC) is composed of multiple copies of several components, namely, pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3), an E3-binding protein (E3BP), and two regulatory components, E1-kinase (PDK) and phospho-E1 phosphatase (PDP).Cited by: 9.
Mutations in the E1alpha subunit of the pyruvate dehydrogenase multienzyme complex may result in congenital lactic acidosis, but little is known about the consequences of these mutations at the enzymatic level.
Here we characterize two mutants (FL and TA) of human pyruvate dehydrogenase in vitro, using the enzyme expressed in Escherichia. We identified a new YS mutation in the X-linked E1 α-PDH gene in a patient with pyruvate dehydrogenase complex (PDHc) deficiency.
The activity in cultured fibroblasts was very low even in the presence of high thiamine pyrophosphate (TPP) concentrations, indicating that the defect could be due to decreased affinity of PDHc for by: 7. A novel null mutation in the pyruvate dehydrogenase phosphatase catalytic subunit gene (PDP1) The mitochondrial multienzyme pyruvate dehydrogenase complex (PDC) irreversibly catalyzes oxidative decarboxylation of pyruvate into acetyl‐CoA as the primary substrate from carbohydrate for the tricarboxylic acid (TCA) cycle and oxidative Author: Jirair K.
Bedoyan, Leah Hecht, Shulin Zhang, Stacey Tarrant, Ann Bergin, Didem Demirbas, Edward Yang. The disease is caused by deficiency of the E1-alpha subunit of the PDH complex related to mutations in the PDHA1 gene (Xp).
Genetic counseling The pattern of inheritance is X-linked. Expert reviewer(s): Dr Garry BROWN - Last update: April 1. Introduction.
The human pyruvate dehydrogenase complex (PDHC) catalyzes the thiamine-dependent decarboxylation of pyruvate, and plays an important role in energy metabolism of the cell since it is an essential and rate-limiting enzyme connecting glycolysis with the tricarboxylic acid cycle and oxidative by:.
The most common cause are mutations in the PDHA1 gene (Xp), which encodes the E1-alpha subunit. Mutations in the genes for the other subunits have been described, but are far less frequent: E1-beta and E2 subunits (PDHB, DLAT); E3 binding protein (PDHX gene); and E3 and PDH phosphatase (DLD and PDP1).
The PDHA1 gene provides instructions for making a protein called E1 alpha. The E1 alpha protein is a piece (a subunit) of a larger protein: two E1 alpha proteins combine with two copies of another protein called E1 beta (produced from the PDHB gene) to form the E1 enzyme.
This enzyme, also known as pyruvate dehydrogenase, is a component of a group of proteins called the pyruvate dehydrogenase.PDHA1 (Pyruvate Dehydrogenase E1 Subunit Alpha 1) is a Protein Coding gene.
Diseases associated with PDHA1 include Pyruvate Dehydrogenase E1-Alpha Deficiency and Leigh Syndrome With its related pathways are Signaling by Retinoic Acid and Citrate cycle (TCA cycle).Gene Ontology (GO) annotations related to this gene include oxidoreductase activity, acting on .