| Name | dopamine beta hydroxylase |
|---|---|
| Synonyms | DBH; DBM; Dopamine beta hydroxylase; Dopamine beta monooxygenase; Dopamine beta hydroxylase precursor; dopamine beta hydroxylase (dopamine beta monooxygenase); DBH; Dopamine beta hydroxylases… |
| Name | cresol |
|---|---|
| CAS | methylphenol |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 3801416 | Kruse LI, DeWolf WE Jr, Chambers PA, Goodhart PJ: Design and kinetic characterization of multisubstrate inhibitors of dopamine beta-hydroxylase. Biochemistry. 1986 Nov 18;25(23):7271-8. |
2(0,0,0,2) | Details |
| 3242615 | DeWolf WE Jr, Carr SA, Varrichio A, Goodhart PJ, Mentzer MA, Roberts GD, Southan C, Dolle RE, Kruse LI: Inactivation of dopamine beta-hydroxylase by isolation and characterization of covalently modified active site peptides. Biochemistry. 1988 Dec 27;27(26):9093-101. Both modified peptides are the same primary sequence: -Pro-Asp-Val---Pro-Gly-Gln-Gln---Tyc-Trp-Cys-Tyr-Va l--- -Pro-Asp-Gly--Pro-Arg, where Tyc is an amino acid residue with the in-chain mass of a cresol-Tyr adduct (106 + 163 Da). |
2(0,0,0,2) | Details |
| 2306476 | Southan C, DeWolf WE Jr, Kruse LI: Inactivation of dopamine beta-hydroxylase by evidence for a second, minor site of covalent modification at 357. Biochim Biophys Acta. 1990 Feb 9;1037(2):256-8. Here we report the recovery and characterization of additional minor peptides that are produced during the inactivation of DBH with p-[3H] cresol. |
2(0,0,0,2) | Details |
| 1868089 | Kim SC, Klinman JP: Mechanism of inhibition of dopamine beta-monooxygenase by and derivatives, as determined by solvent and substrate deuterium isotope effects. Biochemistry. 1991 Aug 20;30(33):8138-44. |
2(0,0,0,2) | Details |
| 3607034 | Goodhart PJ, DeWolf WE Jr, Kruse LI: Mechanism-based inactivation of dopamine beta-hydroxylase by and related alkylphenols. Biochemistry. 1987 May 5;26(9):2576-83. |
2(0,0,0,2) | Details |
| 7893699 | Eipper BA, Quon AS, Mains RE, Boswell JS, Blackburn NJ: The catalytic core of peptidylglycine alpha-hydroxylating monooxygenase: investigation by site-directed mutagenesis, Cu X-ray absorption spectroscopy, and electron paramagnetic resonance. Biochemistry. 1995 Mar 7;34(9):2857-65. A set of mutant PHM proteins whose design was based on the structural and mechanistic similarities of PHM and dopamine beta-monooxygenase (D beta M) was characterized. |
1(0,0,0,1) | Details |