2,3-bisphosphoglycerate 3-phosphatase

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.^[1] This enzyme catalyses the following chemical reaction

2,3-bisphospho-D-glycerate + H₂O

\rightleftharpoons

2-phospho-D-glycerate + phosphate

This reaction is a shortcut in the Luebering-Rapoport pathway.

References

↑ Cho, J., King, J.S., Qian, X., Harwood, A.J. and Shears, S.B. (2008). "Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt". Proc. Natl. Acad. Sci. USA 105: 5998–6003. doi:10.1073/pnas.0710980105. PMID 18413611.

External links

2,3-bisphosphoglycerate 3-phosphatase at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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