Galactose mutarotase

Protein-coding gene in the species Homo sapiens From Wikipedia, the free encyclopedia

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.

AliasesGALM, BLOCK25, GLAT, HEL-S-63p, IBD1, galactose mutarotase (aldose 1-epimerase), galactose mutarotase, GALAC4
External IDsOMIM: 137030; MGI: 2442420; GeneCards: GALM
PDBOrtholog search: PDBe RCSB
Quick facts GALM, Identifiers ...
GALM
Identifiers
AliasesGALM, BLOCK25, GLAT, HEL-S-63p, IBD1, galactose mutarotase (aldose 1-epimerase), galactose mutarotase, GALAC4
External IDsOMIM: 137030; MGI: 2442420; GeneCards: GALM
Available structures
PDBOrtholog search: PDBe RCSB
Enzyme activity
EC #BRENDAExPASyKEGGMetaCyc
5.1.3.3
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_138801

NM_176963

RefSeq (protein)

NP_620156

NP_795937

Location (UCSC)Chr 2: 38.67 – 38.74 MbChr 17: 80.43 – 80.49 Mb
PubMed search[3][4]
Wikidata
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The two main amino acids in the enzyme active site are Glu 304, which acts as a Bronsted-Lowry base and removes a proton, and His 170, which acts as Bronsted-Lowry Acid and donates a proton to the galactose.[7]

References

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