We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00080Copper type II, ascorbate-dependent monooxygenases signatures
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00080
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:
References
| 1 | Authors | Southan C. Kruse L.I. |
| Title | Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain. | |
| Source | FEBS Lett. 255:116-120(1989). | |
| PubMed ID | 2792366 |
| 2 | Authors | Stewart L.C. Klinman J.P. |
| Title | Dopamine beta-hydroxylase of adrenal chromaffin granules: structure and function. | |
| Source | Annu. Rev. Biochem. 57:551-592(1988). | |
| PubMed ID | 3052283 | |
| DOI | 10.1146/annurev.bi.57.070188.003003 |
Copyright
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