Bisphosphoglycerate phosphatase

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bisphosphoglycerate phosphatase
2h4z.jpg
Bisphosphoglycerate phosphatase (bifunctional) homodimer, Human
Identifiers
EC no. 3.1.3.13
CAS no. 9033-04-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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PMC articles
PubMed articles
NCBI proteins

In enzymology, a bisphosphoglycerate phosphatase (EC 3.1.3.13) is an enzyme that catalyzes the chemical reaction

2,3-bisphospho-D-glycerate + H2O 3-phospho-D-glycerate + phosphate

Thus, the two substrates of this enzyme are 2,3-bisphospho-D-glycerate and H2O, whereas its two products are 3-phospho-D-glycerate and phosphate.

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is 2,3-bisphospho-D-glycerate 2-phosphohydrolase. Other names in common use include 2,3-diphosphoglycerate phosphatase, diphosphoglycerate phosphatase, 2,3-diphosphoglyceric acid phosphatase, 2,3-bisphosphoglycerate phosphatase, and glycerate-2,3-diphosphate phosphatase. This enzyme participates in glycolysis/gluconeogenesis.

Structural studies

As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1YFK, 1YJX, 2F90, 2H4X, 2H4Z, 2H52, and 2HHJ.

Related Research Articles

<span class="mw-page-title-main">Bisphosphoglycerate mutase</span> Enzyme

Bisphosphoglycerate mutase is an enzyme expressed in erythrocytes and placental cells. It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-bisphosphoglycerate. BPGM also has a mutase and a phosphatase function, but these are much less active, in contrast to its glycolytic cousin, phosphoglycerate mutase (PGM), which favors these two functions, but can also catalyze the synthesis of 2,3-BPG to a lesser extent.

<span class="mw-page-title-main">Phosphoglycerate mutase</span> Class of enzymes

Phosphoglycerate mutase (PGM) is any enzyme that catalyzes step 8 of glycolysis - the internal transfer of a phosphate group from C-3 to C-2 which results in the conversion of 3-phosphoglycerate (3PG) to 2-phosphoglycerate (2PG) through a 2,3-bisphosphoglycerate intermediate. These enzymes are categorized into the two distinct classes of either cofactor-dependent (dPGM) or cofactor-independent (iPGM). The dPGM enzyme is composed of approximately 250 amino acids and is found in all vertebrates as well as in some invertebrates, fungi, and bacteria. The iPGM class is found in all plants and algae as well as in some invertebrate, fungi, and Gram-positive bacteria. This class of PGM enzyme shares the same superfamily as alkaline phosphatase.

<span class="mw-page-title-main">Fructose-bisphosphate aldolase</span>

Fructose-bisphosphate aldolase, often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism.

Glucose-1,6-bisphosphate synthase is a type of enzyme called a phosphotransferase and is involved in mammalian starch and sucrose metabolism. It catalyzes the transfer of a phosphate group from 1,3-bisphosphoglycerate to glucose-1-phosphate, yielding 3-phosphoglycerate and glucose-1,6-bisphosphate.

In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) (EC 1.2.7.6) is an enzyme that catalyzes the chemical reaction

In enzymology, a guanosine-5'-triphosphate,3'-diphosphate diphosphatase (EC 3.6.1.40) is an enzyme that catalyzes the chemical reaction

In enzymology, a guanosine-diphosphatase (EC 3.6.1.42) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Nucleoside-diphosphatase</span> Group of proteins having nucleoside-diphosphatase activity

In enzymology, a nucleoside-diphosphatase (EC 3.6.1.6) is an enzyme that catalyzes the chemical reaction

In enzymology, an UDP-sugar diphosphatase (EC 3.6.1.45) is an enzyme that catalyzes the chemical reaction

The enzyme 3-phosphoglycerate phosphatase (EC 3.1.3.38) catalyzes the reaction

The enzyme mannosyl-3-phosphoglycerate phosphatase (EC 3.1.3.70) catalyzes the reaction

The enzyme methylphosphothioglycerate phosphatase (EC 3.1.3.14) catalyzes the reaction

The enzyme phosphatidylinositol-3-phosphatase (EC 3.1.3.64) catalyzes the reaction

<span class="mw-page-title-main">Phosphoglycolate phosphatase</span>

Phosphoglycolate phosphatase(EC 3.1.3.18; systematic name 2-phosphoglycolate phosphohydrolase), also commonly referred to as phosphoglycolate hydrolase, 2-phosphoglycolate phosphatase, P-glycolate phosphatase, and phosphoglycollate phosphatase, is an enzyme responsible for catalyzing the conversion of 2-phosphoglycolate into glycolate and phosphate:

The enzyme phosphoserine phosphatase (EC 3.1.3.3) catalyzes the reaction

The enzyme 6-phospho-β-glucosidase (EC 3.2.1.86) catalyzes the following reaction:

<span class="mw-page-title-main">Nicotinate phosphoribosyltransferase</span>

In enzymology, a nicotinate phosphoribosyltransferase (EC 6.3.4.21) is an enzyme that catalyzes the chemical reaction

In enzymology, a glycerate kinase is an enzyme that catalyzes the chemical reaction

2,3-Bisphosphoglycerate 3-phosphatase (EC 3.1.3.80, MIPP1, 2,3-BPG 3-phosphatase) is an enzyme with systematic name 2,3-bisphospho-D-glycerate 3-phosphohydrolase. This enzyme catalyses the following reaction:

Glucosyl-3-phosphoglycerate phosphatase (EC 3.1.3.85, GpgP protein) is an enzyme with systematic name α-D-glucosyl-3-phospho-D-glycerate phosphohydrolase. This enzyme catalyses the following chemical reaction

References