BPGM Human

2,3-Bisphosphoglycerate Mutase (BPGM) is an enzyme that plays a crucial role in the regulation of oxygen release from hemoglobin. It is primarily expressed in erythrocytes (red blood cells) and placental cells . The enzyme is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate . This reaction is essential for modulating the affinity of hemoglobin for oxygen, thereby facilitating oxygen release to tissues.

BPGM is a homodimer, meaning it consists of two identical protein subunits . Each subunit contains six β-strands and ten α-helices, with dimerization occurring along specific faces of these structures . The enzyme’s active site includes important residues such as His-11 and His-188, which are involved in the catalytic process .

The primary function of BPGM is to convert 1,3-bisphosphoglycerate to 2,3-BPG . This conversion is vital for oxygen transport, as 2,3-BPG binds with high affinity to hemoglobin, causing a conformational change that results in the release of oxygen . This mechanism is particularly important in erythrocytes and placental cells, where efficient oxygen delivery is critical .

The production of 2,3-BPG by BPGM is essential for the proper functioning of hemoglobin. 2,3-BPG binds to hemoglobin and reduces its affinity for oxygen, thereby promoting the release of oxygen to tissues . This process is crucial in conditions where oxygen demand is high, such as during physical exertion or in hypoxic environments.

In the placenta, the production of 2,3-BPG facilitates the transfer of oxygen from maternal to fetal hemoglobin . Fetal hemoglobin has a lower affinity for 2,3-BPG, allowing it to bind oxygen more effectively from maternal blood .

Mutations or deficiencies in the BPGM gene can lead to various clinical conditions. For example, a deficiency in BPGM can result in hemolytic anemia, a condition characterized by the destruction of red blood cells . This is because the lack of 2,3-BPG increases the affinity of hemoglobin for oxygen, reducing its ability to release oxygen to tissues .

Additionally, BPGM has been studied in the context of sepsis, where its levels can predict myocardial dysfunction and adverse outcomes . Elevated levels of BPGM in sepsis patients have been associated with increased mortality and cardiac injury .

Human recombinant BPGM is produced using recombinant DNA technology, which involves inserting the BPGM gene into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the enzyme for research and therapeutic purposes. Recombinant BPGM is used in various studies to understand its function and role in different physiological and pathological conditions.