ECM Disulfide formation: sulfhydryl oxidases

[Colin Thorpe]

I wish to advertise a newly-discovered family of enzymes involved in
disulfide bond formation in secreted proteins and peptides. My hope is
that someone in the Drosophila community might be interested in
following them up.

These sulfhydryl oxidases are found in all multicellular organisms. 
They are not found in yeast.  The human counterparts have been called
"bone-derived growth factor", "cell inhibitory factor" and "quiescin".  

Drosophila has 3 or 4 such sulfhydryl oxidases genes (CG4670-PA;
CG17843; CG6690-PA;  CG31413-PA).  Their roles are unknown.

Circumstantial (non-knock-out) evidence in mammals suggests involvement
in ECM formation and differentiation, in spermatogenesis, and in
secretion of peptides and proteins.  

For a recent review on these enzymes, and some nice pictures of cellular
distribution in human tissues, see:  

"Sulfhydryl oxidases: emerging catalysts of protein disulfide bond
formation in eukaryotes" (2002)  Thorpe et al.  Archives of Biochemistry
and Biophysics 405, 1-12.  

Thank you.

Colin Thorpe

Professor of Biochemistry                                        
Department of Chemistry and Biochemistry           
University of Delaware                                              
Newark, Delaware  19716
 Phone:  (302) 831-2689 (FAX -6335)
http://www.udel.edu/chem/thorpe/
---