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Domain

The protein goes through several conformation states during the reaction cycle, giving rise to hysteresis. In the initial state, the ligand-free protein is in an inactive conformation (E*). Substrate binding triggers a change to the active conformation (E). UDP-xylose binding triggers the transition to a distinct, inhibited conformation. The presence of an intrinsically disordered C-terminus promotes a more dynamic protein structure and favors a conformation with high affinity for UPD-xylose.

The allosteric switch region moves by about 5 Angstroms when UDP-xylose is bound, and occupies part of the UDP-glucose binding site. At the same time it promotes domain movements that disrupt the active hexameric ring structure and lead to the formation of a horseshoe-shaped, inactive hexamer.

Function

Catalyzes the formation of UDP-alpha-D-glucuronate, a constituent of complex glycosaminoglycans (PubMed:21502315, PubMed:21961565, PubMed:22123821, PubMed:23106432, PubMed:25478983, PubMed:27966912, PubMed:30420606, PubMed:30457329). Required for the biosynthesis of chondroitin sulfate and heparan sulfate. Required for embryonic development via its role in the biosynthesis of glycosaminoglycans (By similarity). Required for proper brain and neuronal development (PubMed:32001716).

Involvement in disease

Developmental and epileptic encephalopathy 84

DEE84

A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE84 is an autosomal recessive form characterized by onset of refractory seizures in the first months of life.

None

The disease is caused by variants affecting the gene represented in this entry.

Pathway

Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.

Sequence similarities

Belongs to the UDP-glucose/GDP-mannose dehydrogenase family.

Tissue specificity

Detected in heart, placenta, liver, pancreas, spleen, thymus, prostate, ovary, small intestine and colon (PubMed:9737970). Widely expressed (PubMed:9737970).

Alternative names

UDP-glucose 6-dehydrogenase, UDP-Glc dehydrogenase, UDP-GlcDH, UDPGDH, UGDH

Target type

Proteins

Primary research area

Oncology

Molecular weight

55024Da

We found 1 product in 1 category

Proteins & Peptides

Target

Species of origin

Search our catalogue for 'UGDH' (1)

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