Galactose mutarotase explained

Galactose mutarotase (aldose 1-epimerase) (gene name GALM) is a human enzyme that reversibly converts α-aldose to the β-anomer.^[1] This enzyme catalyzes the first step of the Leloir pathway, which is involved in galactose metabolism.^[2] It belongs to family of aldose epimerases.

The two main amino acids in the enzyme active site are Glu 304, which acts as a Bronsted-Lowry base and abstracts a proton, and His 170, which acts as Bronsted-Lowry Acid to donate a proton to the galactose.^[3]

External links

• PDBe-KB provides an overview of all the structure information available in the PDB for Human Aldose 1-epimerase (Galactose mutarotase)

Notes and References

1. Thoden JB, Timson DJ, Reece RJ, Holden HM . Molecular structure of human galactose mutarotase . English . The Journal of Biological Chemistry . 279 . 22 . 23431–23437 . May 2004 . 15026423 . 10.1074/jbc.M402347200 . free .
2. Holden HM, Rayment I, Thoden JB . Structure and function of enzymes of the Leloir pathway for galactose metabolism . The Journal of Biological Chemistry . 278 . 45 . 43885–43888 . November 2003 . 12923184 . 10.1074/jbc.R300025200 . Ivan Rayment . free .
3. Thoden JB, Kim J, Raushel FM, Holden HM . The catalytic mechanism of galactose mutarotase . Protein Science . 12 . 5 . 1051–1059 . May 2003 . 12717027 . 2323875 . 10.1110/ps.0243203 .