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 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.[7]
^ abcGRCh38: Ensembl release 89: ENSG00000143891 – Ensembl, May 2017
^ abcGRCm38: 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. PMC 2323875. PMID 12717027.
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Galactosemutarotase (aldose 1-epimerase) (gene name GALM) is a human enzyme that reversibly converts α-aldose to the β-anomer. This enzyme catalyzes the...
converts β-D-galactose to UDP-glucose. The initial stage is the conversion of β-D-galactose to α-D-galactose by the enzyme, mutarotase (GALM). The Leloir...
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the catabolism of D-galactose. It is named after Luis Federico Leloir, who first described it. In the first step, galactosemutarotase facilitates the conversion...
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structural genes: galE (epimerase), galT (galactose transferase), galK (galactokinase), and galM (mutarotase) which are transcribed from two overlapping...
(MeSH) Portal: Biology Beebe, Jane A.; Frey, Perry A. (1998-10-01). "GalactoseMutarotase: Purification, Characterization, and Investigations of Two Important...
Wikimedia Commons Beebe, Jane A.; Frey, Perry A. (1998-10-01). "GalactoseMutarotase: Purification, Characterization, and Investigations of Two Important...
PMID 29409891. v t e Beebe, Jane A.; Frey, Perry A. (1998-10-01). "GalactoseMutarotase: Purification, Characterization, and Investigations of Two Important...
Portal: Biology v t e Beebe, Jane A.; Frey, Perry A. (1998-10-01). "GalactoseMutarotase: Purification, Characterization, and Investigations of Two Important...
page in the UCSC Genome Browser. Beebe JA, Frey PA (1998-10-01). "GalactoseMutarotase: Purification, Characterization, and Investigations of Two Important...
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Portal: Biology v t e Beebe, Jane A.; Frey, Perry A. (1998-10-01). "GalactoseMutarotase: Purification, Characterization, and Investigations of Two Important...
ISBN 9781608314126. Portal: Biology Beebe, Jane A.; Frey, Perry A. (1998-10-01). "GalactoseMutarotase: Purification, Characterization, and Investigations of Two Important...
uk/interpro/IEntry?ac=IPR016305 Beebe, Jane A.; Frey, Perry A. (1998-10-01). "GalactoseMutarotase: Purification, Characterization, and Investigations of Two Important...
Portal: Biology v t e Beebe, Jane A.; Frey, Perry A. (1998-10-01). "GalactoseMutarotase: Purification, Characterization, and Investigations of Two Important...
beta-scruin, in galactose oxidase from the fungus Dactylium dendroides, and in the Escherichia coli NanM protein, a sialic acid mutarotase. The structure...
gene sequences encoding aldose-1-epimerases that act as sulfoquinovose mutarotases, catalyzing the interconversion of the α and β anomers of sulfoquinovose...