人 PDP1 抗体对
01AB01550
Pyruvate dehydrogenase phosphatase catalytic subunit 1 (PDP1) is an essential enzyme within the pyruvate dehydrogenase complex (PDC), where it catalyzes the dephosphorylation and activation of pyruvate dehydrogenase (E1). This process is critical for converting pyruvate into acetyl-CoA, a key molecule in cellular energy production via the citric acid cycle. PDP1 belongs to the PPM family of serine/threonine phosphatases and requires magnesium ions for its catalytic activity. Its function is enhanced by calcium-dependent binding to the lipoyl domain of dihydrolipoyl acetyltransferase (E2), which is part of PDC. Structural studies reveal a conserved central β-sandwich core and unique surface features that confer specificity for PDC components. Mutations in the PDP1 gene can lead to pyruvate dehydrogenase deficiency, a rare condition characterized by lactic acidosis, developmental delays, and neurological impairments. This occurs due to impaired PDC activity, reducing cellular energy production and causing toxic metabolite buildup.
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技术参数
- 靶点基因名
- PDP1
- 基因别名
- PDP; PPM2C
- 蛋白别名
- pyruvate dehydrogenase phosphatase catalytic subunit 1; PDP1
- UniProt
- Q9P0J1
- 物种
- Human
产品详情
- 靶点名称
- PDP1
- 蛋白名称
- pyruvate dehydrogenase phosphatase catalytic subunit 1
- 蛋白别名
- [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1; mitochondrial; PDP 1; Protein phosphatase 2C; Pyruvate dehydrogenase phosphatase catalytic subunit 1; PDPC 1
- 靶点基因名
- PDP1
- 基因别名
- PDP; PPM2C
- UniProt
- Q9P0J1
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Pyruvate dehydrogenase phosphatase catalytic subunit 1 (PDP1) is an essential enzyme within the pyruvate dehydrogenase complex (PDC), where it catalyzes the dephosphorylation and activation of pyruvate dehydrogenase (E1). This process is critical for converting pyruvate into acetyl-CoA, a key molecule in cellular energy production via the citric acid cycle. PDP1 belongs to the PPM family of serine/threonine phosphatases and requires magnesium ions for its catalytic activity. Its function is enhanced by calcium-dependent binding to the lipoyl domain of dihydrolipoyl acetyltransferase (E2), which is part of PDC. Structural studies reveal a conserved central β-sandwich core and unique surface features that confer specificity for PDC components. Mutations in the PDP1 gene can lead to pyruvate dehydrogenase deficiency, a rare condition characterized by lactic acidosis, developmental delays, and neurological impairments. This occurs due to impaired PDC activity, reducing cellular energy production and causing toxic metabolite buildup.