Sequence similarity between dopamine β‐hydroxylase and peptide α‐amidating enzyme: Evidence for a conserved catalytic domain

Southan, Christopher; Kruse, Lawrence I.

doi:10.1016/0014-5793(89)81072-5

Cited by 73 publications

(38 citation statements)

References 19 publications

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“…was purified from bovine adrenal medullae and has been well characterized both kinetically and physicochemically (reviewed by Stewart and Klinman [24]). In addition, the high similarity of nucleotide and amino acid sequence between AE-I and DBH in the putative copper-binding sites also supports the similarity of the two enzymes in the reaction mechanism [28]. In the present study, we focused on a frog PHM (AE-I) as a hydroxylating enzyme.…”

Section: Discussionsupporting

confidence: 52%

Characterization of a Xenopus laevis skin peptidylglycine α‐hydroxylating monooxygenase expressed in insect‐cell culture

Shimoi

Kawahara

Suzuki

et al. 1992

European Journal of Biochemistry

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The C-terminal amide structure of peptide hormones and neurotransmitters is synthesized via a two-step reaction catalyzed by peptidylglycine a-hydroxylating monooxygenase (PHM) and peptidylhydroxyglycine N-C lyase. A Xenopus laevis PHM expressed in insect-cell culture by the baculovirus-expression-vector system was purified to homogeneity and characterized. Using a newly established assay system for PHM, the kinetic features of this enzyme were investigated. As expected, the enzyme required copper ions, L-ascorbate and molecular oxygen for turnover. Salts like KI and KCI, and catalase stabilized the enzyme in the presence of L-ascorbate. The optimum pH value for the enzyme reaction was around six when Mes buffer was used and around seven when phosphate buffer was used under the same assay condition. Below pH 6, acetate, iodide and chloride ions activated the reaction. The kinetic analysis is consistent with a ping-pong mechanism with respect to peptide and L-ascorbate, and the peptide showed substrate inhibition. The substrate specificity of the enzyme at the penultimate position was examined by competitive assay using tripeptides with glycine at the C-termini and the inhibitory potency of these peptides in descending order was methionine > aromatic > non-polar amino acids.

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Section: Discussionsupporting

confidence: 52%

Characterization of a Xenopus laevis skin peptidylglycine α‐hydroxylating monooxygenase expressed in insect‐cell culture

Shimoi

Kawahara

Suzuki

et al. 1992

European Journal of Biochemistry

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“…Nucleotide sequence data reported are available in the Third Party Annotation section of the DDBJ/EMBL/GenBank databases under the accession number TPA: BK005823. The deduced amino acid sequence for AmT␤h indicated an ORF of 613 amino acids constituting a protein with a molecular mass of 70.09 kDa (Fig.·4) (Southan and Kruse, 1989). In addition, 14 cysteine residues are responsible for intra-and intermolecular disulfide linkages in bovine D␤h (Robertson et al, 1994), and 12 of these cysteine residues are located in similar positions in the AmT␤H protein.…”

Section: T␤h Sequencementioning

confidence: 99%

Division of labor in the honey bee (Apis mellifera): the role of tyramine β-hydroxylase

Lehman

Schulz

Barron

et al. 2006

Journal of Experimental Biology

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SUMMARY The biogenic amine octopamine (OA) is involved in the regulation of honey bee behavioral development; brain levels are higher in foragers than bees working in the hive, especially in the antennal lobes, and treatment causes precocious foraging. We measured brain mRNA and protein activity of tyramineβ-hydroxylase (T βh), an enzyme vital for OA synthesis, in order to begin testing the hypothesis that this enzyme is responsible for the rising levels of OA during honey bee behavioral development. Brain OA levels were greater in forager bees than in bees engaged in brood care, as in previous studies, but T βh activity was not correlated with bee behavior. Tβh mRNA levels, however, did closely track OA levels during behavioral development, and T βh mRNA was localized to previously identified octopaminergic neurons in the bee brain. Our results show that the transcription of this neurotransmitter synthetic enzyme is associated with regulation of social behavior in honey bees, but other factors may be involved.

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“…1B) (6,14). Interestingly, this region contains four conserved disulfide bridges and six conserved copper ligands (15,16).…”

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confidence: 99%

Cell Type-specific Storage of Dopamine β-Monooxygenase

Oyarce

Eipper

2000

Journal of Biological Chemistry

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Expression of dopamine ␤-monooxygenase (DBM), the enzyme that converts dopamine into norepinephrine, is limited to adrenal chromaffin cells and a small population of neurons. We studied DBM trafficking to regulated granules by stably expressing rat DBM in AtT-20 corticotrope tumor cells, which contain regulated granules, and in Chinese hamster ovary (CHO) cells, which lack regulated granules. The behavior of exogenous DBM in both cell lines was compared with endogenous DBM in adrenal chromaffin cells. CHO cells secreted active DBM, indicating that production of active enzyme does not require features unique to neuroendocrine cells. Pulse-chase experiments indicated that early steps in DBM maturation followed a similar time course in AtT-20, CHO, and adrenal chromaffin cells. Use of a conformation-sensitive DBM antiserum indicated that acquisition of a folded structure occurred with a similar time course in all three cell types. Cell type-specific differences in DBM trafficking became apparent only when storage in granules was examined. As expected, DBM was stored in secretory granules in chromaffin cells; CHO cells failed to store DBM. Despite the fact that AtT-20 cells have regulated granules, exogenous DBM was not stored in these granules. Thus storage of DBM in secretory granules requires cell type specific factors.

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Sequence similarity between dopamine β‐hydroxylase and peptide α‐amidating enzyme: Evidence for a conserved catalytic domain

Cited by 73 publications

References 19 publications

Characterization of a Xenopus laevis skin peptidylglycine α‐hydroxylating monooxygenase expressed in insect‐cell culture

Characterization of a Xenopus laevis skin peptidylglycine α‐hydroxylating monooxygenase expressed in insect‐cell culture

Division of labor in the honey bee (Apis mellifera): the role of tyramine β-hydroxylase

Cell Type-specific Storage of Dopamine β-Monooxygenase

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