Literature summary for 5.4.2.4 extracted from

Garel, M.C.; Joulin, V.; Le Boulch, P.; Calvin, M.C.; Prehu, M.O.; Arous, N.; Longin, R.; Rosa, R.; Rosa, J.; Cohen-Solal, M.
Human bisphosphglycerate mutase. Expression in Escherichia coli and use of site-directed mutagenesis in the evaluation of the role of the carboxyl-terminal region in the enzymatic mechanism (1989), J. Biol. Chem., 264, 18966-18972.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
additional information	a minimal deletion of 7 amino acids from the C-terminus completely abolishes all catalytic activities	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
erythrocyte	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1,3-Diphosphoglycerate	the enzyme has additional activities of EC 5.4.2.1(phosphoglycerate mutase) and EC 3.1.3.13 (bisphosphoglycerate phosphatase)	Homo sapiens	2,3-Diphosphoglycerate	-	?
1,3-Diphosphoglycerate	multifunctional enzyme for synthesis and degradation of 2,3-diphosphoglycerate	Homo sapiens	2,3-Diphosphoglycerate	-	?

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Release 2023.1 (January 2023)