Galactose mutarotase (aldose 1-epimerase) (gene name GALM) is a human enzyme that reversibly converts α-aldose to the β-anomer.[5] This enzyme catalyzes the first step of the Leloir pathway, which is involved in galactose metabolism.[6] It belongs to family of aldoseepimerases.
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.[7]
References
^ a b cGRCh38: Ensembl release 89: ENSG00000143891 – Ensembl, May 2017
^ a b cGRCm38: Ensembl release 89: ENSMUSG00000035473 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Thoden JB, Timson DJ, Reece RJ, Holden HM (May 2004). "Molecular structure of human galactose mutarotase". The Journal of Biological Chemistry. 279 (22): 23431–23437. doi:10.1074/jbc.M402347200. PMID 15026423.
^Holden HM, Rayment I, Thoden JB (November 2003). "Structure and function of enzymes of the Leloir pathway for galactose metabolism". The Journal of Biological Chemistry. 278 (45): 43885–43888. doi:10.1074/jbc.R300025200. PMID 12923184.
^Thoden JB, Kim J, Raushel FM, Holden HM (May 2003). "The catalytic mechanism of galactose mutarotase". Protein Science. 12 (5): 1051–1059. doi:10.1110/ps.0243203. PMC2323875. PMID 12717027.
External links
PDBe-KB provides an overview of all the structure information available in the PDB for Human Aldose 1-epimerase (Galactose mutarotase)