Galactose mutarotase

Protein-coding gene in the species Homo sapiens

GALM

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1SNZ, 1SO0

Identifiers

Aliases

GALM, BLOCK25, GLAT, HEL-S-63p, IBD1, galactose mutarotase (aldose 1-epimerase), galactose mutarotase, GALAC4

External IDs

OMIM: 137030; MGI: 2442420; HomoloGene: 71795; GeneCards: GALM; OMA:GALM - orthologs

Gene location (Human)

Chr.	Chromosome 2 (human)^[1]

Band	2p22.1	Start	38,666,081 bp^[1]
Band	2p22.1	End	38,741,237 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 17 (mouse)^[2]

Band	17\|17 E3	Start	80,434,900 bp^[2]
Band	17\|17 E3	End	80,492,530 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

right adrenal gland

pancreatic ductal cell

left adrenal gland

duodenum

right uterine tube

renal medulla

jejunal mucosa

kidney

rectum

vena cava

Top expressed in

olfactory epithelium

lacrimal gland

left lobe of liver

epithelium of stomach

jejunum

gallbladder

superior surface of tongue

intestinal epithelium

kidney

duodenum

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	isomerase activity aldose 1-epimerase activity carbohydrate binding catalytic activity
Cellular component	extracellular exosome cytoplasm
Biological process	hexose metabolic process glucose metabolic process galactose metabolic process galactose catabolic process via UDP-galactose carbohydrate metabolic process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


130589


319625

Ensembl


ENSG00000143891


ENSMUSG00000035473

UniProt


Q96C23


Q8K157

RefSeq (mRNA)


NM_138801


NM_176963

RefSeq (protein)


NP_620156


NP_795937

Location (UCSC)

Chr 2: 38.67 – 38.74 Mb

Chr 17: 80.43 – 80.49 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

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]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000143891 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: 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.