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PROSITE documentation PDOC00080 [for PROSITE entry PS00085]

Copper type II, ascorbate-dependent monooxygenases signatures





Description

Copper type II, ascorbate-dependent monooxygenases [1] are a class of enzymes that requires copper as a cofactor and which uses ascorbate as an electron donor. The enzymes which belong to this category are:

  • Dopamine-β-monooxygenase (EC 1.14.17.1) (DBH) [2], which catalyzes the conversion of dopamine to the neurotransmitter norepinephrine.
  • Peptidyl-glycine α-amidating monooxygenase (EC 1.14.17.3) (PAM), which catalyzes the conversion of the carboxy-terminal glycine of many active peptides and hormones to an amide group.

There are a few regions of sequence similarities between these two enzymes, two of these regions contain clusters of conserved histidine residues which are most probably involved in binding copper. We selected these two regions as signature patterns.

Last update:

May 2004 / Text revised.

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Technical section

PROSITE methods (with tools and information) covered by this documentation:

CU2_MONOOXYGENASE_2, PS00085; Copper type II, ascorbate-dependent monooxygenases signature 2  (PATTERN)

CU2_MONOOXYGENASE_1, PS00084; Copper type II, ascorbate-dependent monooxygenases signature 1  (PATTERN)


References

1AuthorsSouthan C. Kruse L.I.
TitleSequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain.
SourceFEBS Lett. 255:116-120(1989).
PubMed ID2792366

2AuthorsStewart L.C. Klinman J.P.
TitleDopamine beta-hydroxylase of adrenal chromaffin granules: structure and function.
SourceAnnu. Rev. Biochem. 57:551-592(1988).
PubMed ID3052283
DOI10.1146/annurev.bi.57.070188.003003



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