Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (PDHB)
The protein contains 359 amino acids for an estimated molecular weight of 39233 Da.
The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle. (updated: April 1, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
Biological Process
Acetyl-CoA biosynthetic process from pyruvate
Cellular metabolic process
Cellular nitrogen compound metabolic process
Glucose metabolic process
Mitochondrial acetyl-CoA biosynthetic process from pyruvate
Pyruvate metabolic process
Regulation of acetyl-CoA biosynthetic process from pyruvate
Small molecule metabolic process
Tricarboxylic acid cycle
The reference OMIM entry for this protein is 179060
Pyruvate dehydrogenase, beta polypeptide; pdhb
Pyruvate dehydrogenase complex, e1 beta polypeptide; phe1b
DESCRIPTION
Pyruvate dehydrogenase is a tetramer consisting of 2 alpha subunits (PDHA1; 300502) and 2 beta subunits (PDHB). The enzyme, which is found in mitochondria, is one of the component enzymes of the pyruvate dehydrogenase multienzyme complex (PDH). It catalyzes the first reaction of an oxidative decarboxylation sequence converting pyruvate to acetyl-CoA and CO(2) (summary by Koike et al., 1988).CLONING
Koike et al. (1988) cloned and sequenced cDNAs encoding the alpha and the beta subunits. Ho et al. (1988) isolated a 1.5-kb cDNA clone for the beta subunit of E1 from a human liver gamma-gt11 cDNA library using anti-E1 serum.MAPPING
Using a cDNA probe, Olson et al. (1990) demonstrated that the PHE1B gene is located on 3p13-q23.GENE STRUCTURE
Koike et al. (1990) described the molecular cloning of the entire human PHE1B gene, its characterization by restriction enzyme analysis, and its complete nucleotide sequence. The PHE1B gene contains 10 exons. All intron-exon splice junctions follow the GT/AG rule. The Alu family was found in introns 2 and 8.MOLECULAR GENETICS
In 2 unrelated patients with pyruvate dehydrogenase deficiency (PDHBD; 614111), Brown et al. (2004) identified homozygous mutations in the PDHB gene (179060.0001-179060.0002). The patients presented with lactic acidosis and neurologic dysfunction and had little residual PDH activity in cultured fibroblasts. The consequences of the mutations could be analyzed by comparison with the normal structure of the human PDH E1 enzyme. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 179060 was added.