1he3
|
HUMAN BILIVERDIN IX BETA REDUCTASE: NADP/MESOBILIVERDIN IV ALPHA TERNARY COMPLEX
OverviewOverview
Biliverdin IXbeta reductase (BVR-B) catalyzes the pyridine, nucleotide-dependent production of bilirubin-IXbeta, the major heme, catabolite during early fetal development. BVR-B displays a preference for, biliverdin isomers without propionates straddling the C10 position, in, contrast to biliverdin IXalpha reductase (BVR-A), the major form of BVR in, adult human liver. In addition to its tetrapyrrole clearance role in the, fetus, BVR-B has flavin and ferric reductase activities in the adult. We, have solved the structure of human BVR-B in complex with NADP+ at 1.15 A, resolution. Human BVR-B is a monomer displaying an alpha/beta dinucleotide, binding fold. The structures of ternary complexes with mesobiliverdin, IValpha, biliverdin IXalpha, FMN and lumichrome show that human BVR-B has, a ... [(full description)]
About this StructureAbout this Structure
1HE3 is a [Single protein] structure of sequence from [Homo sapiens] with NAP and MBV as [ligands]. Active as [[1]], with EC number [1.3.1.24]. Full crystallographic information is available from [OCA].
ReferenceReference
Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme., Pereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M, Nat Struct Biol. 2001 Mar;8(3):215-20. PMID:11224564
Page seeded by OCA on Mon Oct 29 21:04:23 2007
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Homo sapiens
- Single protein
- Coll, M.
- Cunningham, O.
- Darcy, K.
- Macedo-Ribeiro, S.
- Mantle, T.J.
- Parraga, A.
- Pereira, P.J.B.
- Perez-Luque, R.
- MBV
- NAP
- Alpha/beta dinucleotide binding fold
- Biliverdin-ix beta reductase
- Diaphorase
- Flavin reductase
- Foetal metabolism
- Green haem binding protein
- Haem degradation
- Methaemoglobin reductase