Disease relevance of GALM

• Sequence analysis indicates that the yeast epimerase has an N-terminal domain (residues 1-377) that shows significant similarity with Escherichia coli and human UDPgalactose 4-epimerase, and a C-terminal domain (residues 378-699), which shows extensive identity to either the bacterial or human aldose 1-epimerase (mutarotase) [1].

High impact information on GALM

• Galactose mutarotase catalyzes the conversion of beta-d-galactose to alpha-d-galactose during normal galactose metabolism [2].
• Molecular structure of human galactose mutarotase [2].
• Aldose 1-epimerase or mutarotase (EC 5.1.3.3) is a key enzyme of carbohydrate metabolism catalysing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose [3].
• These results demonstrate that the S. cerevisiae UDPgalactose 4-epimerase is a bifunctional enzyme with aldose 1-epimerase activity [1].
• OBJECTIVE: To determine if the discrepancy between gestational age estimated by last menstrual period and by biparietal diameter (GALMP - GABPD) is associated with adverse pregnancy outcome [4].

Chemical compound and disease context of GALM

• In order to show the kind of information accessible with this type of technique, we give an example: the conformational study of the galactose mutarotase from Escherichia coli, an enzyme involved in the galactose metabolism [5].

Associations of GALM with chemical compounds

• Here we report the x-ray crystallographic analysis of human galactose mutarotase both in the apoform and complexed with its substrate, beta-d-galactose [2].

Other interactions of GALM

• The risk of death was a factor of 6.1 higher if GALMP - GABPD of > or = 8 days was combined with increased (> 2 x multiple of median) maternal alpha-fetoprotein measured in the 2nd trimester [4].

References