Type | Description |
---|---|
Definition | CYP4B1-like isozyme short form |
Date | Results | Publications |
---|---|---|
2019-02-09 10:51:00 | This study concluded that the interplay of noncovalent protein-directed heme deformation and a confined and rigidified active site due to covalent linkage of the heme to the protein are the primary features that confer omega-regioselectivity in 4B1 oxidations. | 29858244 |
2017-06-24 11:34:00 | P450 4B1 exhibits structural adaptations for omega-hydroxylation that include changes in the conformation of the heme and changes in a highly conserved helix I motif that is associated with selective oxygenation of unactivated primary C-H bonds. | 28167536 |
2017-06-24 11:14:00 | A co-crystal structure of the rabbit family 4 enzyme CYP4B1 with its substrate octane reveals that the propensity for omega-hydroxylation is orchestrated by active-site sterics, partially mediated by an unusual heme-polypeptide ester bond. | 28363936 |
2017-06-10 12:42:00 | spectral binding affinities and oxidative metabolism of the furan analogs by the purified recombinant CYP4B1 variants were analyzed: the naturally occurring perilla ketone was found to be the tightest binder to CYP4B1, but also the analog that was most extensively metabolized by oxidative processes to numerous non-reactive reaction products. | 28073960 |
2015-04-18 12:42:00 | A proline residue in the meander region at position 427 in human CYP4B1 and 422 in rabbit CYP4B1 is important for protein stability and rescues the 4-ipomeanol bioactivation. | 25247810 |
Type | IDs |
---|---|
Gene |
UniProtKB-ID:
CP4B1_RABIT
UniprotKB:
P15128
UniParc:
UPI00001281E1
EMBL:
AF332576,
AF176914,
M29852
KO:
ocu:100008805
|
Nucleutide sequences |
EMBL-CDS:
AAG52885.1,
AAA31214.1,
AAD52658.4
|
Protein sequencees |
RefSeq:
NP_001075572.1
|
Others |
UniRef100:
UniRef100_P15128
UniRef90:
UniRef90_P15128
UniRef50:
UniRef50_P13584
UniGene:
Ocu.1854
|
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