Literature summary extracted from

Kensil, C.R.; Hediger, M.A.; Ozols, J.; Strittmatter, P.
Isolation and partial characterization of the NH2-terminal membrane-binding domain of NADH-cytochrome b5 reductase (1983), J. Biol. Chem., 258, 14656-14663.

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.6.2.2	Bos taurus	-	-	-

Posttranslational Modification

EC Number	Posttranslational Modification	Comment	Organism
1.6.2.2	lipoprotein	amphipathic membrane protein containing a hydrophilic, catalytic domain and a smaller hydrohobic membrane-binding domain	Bos taurus

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.6.2.2	separation of membrane binding and catalytic domain	Bos taurus

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
1.6.2.2	liver	-	Bos taurus	-

Subunits

EC Number	Subunits	Comment	Organism
1.6.2.2	More	liver: membrane binding domain located at NH2-terminal site of protein, 6400-6500 Da	Bos taurus

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.6.2.2	NADH	-	Bos taurus

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)