Function
Galactose mutarotase (GalM) reversibly converts α-lactose to β-lactose. GalM catalyzes the first step in galactose metabolism[1].
Structural highlights
From extensive study of mutations in Lactococcus lactis GalM complexes with various sugars it was found that residues H170 and E304 are critical for the active site binding.
3D structures of galactose mutarotase
Updated on 03-March-2016
1l7j – LlGalM – Lactococcus lactis
1l7k, 1ns0, 1ns2, 1ns8, 1nsu, 1nsx – LlGalM (mutant) + α-D-galactose
1mmu, 1ns4, 1ns7, 1nsr, 1nss, 1nsv – LlGalM (mutant) + β-D-glucose
1nsz – LlGalM (mutant) + α-D-glucose
1mmx – LlGalM (mutant) + α-L-fuccose
1mmy – LlGalM (mutant) + D-quinovose
1mmz – LlGalM (mutant) + β-L-arabinose
1mn0 – LlGalM (mutant) + D-xylose
1nsm – LlGalM (mutant) + α-D-galactose + β-D-galactose
1lur – GalM – Caenorhabditis elegans
1snz – hGalM – human
1so0 - hGalM (mutant) + α-D-galactose
3mwx - GalM – Bacillus subtilis
3nre – GalM – Escherichia coli
References
- ↑ Thoden JB, Kim J, Raushel FM, Holden HM. The catalytic mechanism of galactose mutarotase. Protein Sci. 2003 May;12(5):1051-9. PMID:12717027
