Literature summary extracted from

Rose, R.B.; Pullen, K.E.; Bayle, J.H.; Crabtree, G.R.; Alber, T.
Biochemical and structural basis for partially redundant enzymatic and transcriptional functions of DCoH and DCoH2 (2004), Biochemistry, 43, 7345-7355.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
4.2.1.96	hanging-drop vapor diffusion method at 4°C, 1.6 A resolution crystal structure, space group P3(1)21, unit cell length: a = b = 57.92 A, c = 114.63 A	Mus musculus

Organism

EC Number	Organism	UniProt	Comment	Textmining
4.2.1.96	Mus musculus	Q9CZL5	DcoH2 (dimerization cofactor of HNF1alpha)	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
4.2.1.96	DcoH2 (dimerization cofactor of HNF1alpha)	Mus musculus

Subunits

EC Number	Subunits	Comment	Organism
4.2.1.96	tetramer	DcoH2 (dimerization cofactor of HNF1alpha), forms a tetramer, readily disproportionates and forms a 2:2 complex with HNF1 in vitro	Mus musculus

Synonyms

EC Number	Synonyms	Comment	Organism
4.2.1.96	DcoH2	dimerization cofactor of HNF1alpha	Mus musculus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)