bisphosphoglycerate phosphatase | |||||||||
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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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In enzymology, a bisphosphoglycerate phosphatase (EC 3.1.3.13) is an enzyme that catalyzes the chemical reaction
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.
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.
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.
In enzymology, a glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) (EC 1.2.7.6) is an enzyme that catalyzes the chemical reaction
In enzymology, a S-methyl-5-thioribose-1-phosphate isomerase is an enzyme that catalyzes the chemical reaction
In enzymology, a phosphoribosylformylglycinamidine synthase (EC 6.3.5.3) is an enzyme that catalyzes the chemical reaction
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The enzyme threonine synthase (EC 4.2.3.1) 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 nucleotide diphosphatase (EC 3.6.1.9) is an enzyme that catalyzes the chemical reaction
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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:
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The enzyme 6-phospho-β-glucosidase (EC 3.2.1.86) catalyzes the following reaction:
In enzymology, a nicotinate-nucleotide diphosphorylase (carboxylating) (EC 2.4.2.19) is an enzyme that catalyzes the chemical reaction
In enzymology, a nicotinate phosphoribosyltransferase (EC 6.3.4.21) is an enzyme that catalyzes the chemical reaction
In enzymology, a gluconokinase is an enzyme that catalyzes the chemical reaction
In enzymology, a glycerate kinase is an enzyme that catalyzes the chemical reaction
In enzymology, a polynucleotide 5'-hydroxyl-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: