Galactose mutarotase

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
Gene location (Human)
Chr.	Chromosome 2 (human)
End	38,741,237 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	80,492,530 bp
RNA expression pattern
	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
	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
	130589
	319625
	ENSG00000143891
	ENSMUSG00000035473
	Q96C23
	Q8K157
	NM_138801
	NM_176963
	NP_620156
	NP_795937
	Wikidata
View/Edit Human	View/Edit Mouse

Galactose mutarotase (aldose 1-epimerase) (gene name GALM) is a human enzyme that converts alpha-aldose to the beta-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

1 2 3 GRCh38: Ensembl release 89: ENSG00000143891 - Ensembl, May 2017
1 2 3 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.

External links

PDBe-KB provides an overview of all the structure information available in the PDB for Human Aldose 1-epimerase (Galactose mutarotase)

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000143891 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000035473 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] 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.

[6] 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.

[7] 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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