{PDOC00080}
{PS00084; CU2_MONOOXYGENASE_1}
{PS00085; CU2_MONOOXYGENASE_2}
{BEGIN}
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* Copper type II, ascorbate-dependent monooxygenases signatures *
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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-beta-monooxygenase (EC 1.14.17.1)  (DBH) [2], which  catalyzes the
   conversion of dopamine to the neurotransmitter norepinephrine.
 - Peptidyl-glycine alpha-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.

-Consensus pattern: H-H-M-x(2)-F-x-C
                    [The 2 H's are copper ligands]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Consensus pattern: H-x-F-x(4)-H-T-H-x(2)-G
                    [The 3 H's are copper ligands]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: May 2004 / Text revised.

[ 1] Southan C., Kruse L.I.
     "Sequence similarity between dopamine beta-hydroxylase and peptide
     alpha-amidating enzyme: evidence for a conserved catalytic domain."
     FEBS Lett. 255:116-120(1989).
     PubMed=2792366
[ 2] Stewart L.C., Klinman J.P.
     "Dopamine beta-hydroxylase of adrenal chromaffin granules: structure
     and function."
     Annu. Rev. Biochem. 57:551-592(1988).
     PubMed=3052283; DOI=10.1146/annurev.bi.57.070188.003003

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