Enzymes of the Xanthine Oxidase Family: The Role of Molybdenum

2002 ◽  
pp. 363-380
Keyword(s):  
Xanthine Oxidase ◽  
Xanthine Oxidase Family

scholarly journals The Role of System-Specific Molecular Chaperones in the Maturation of Molybdoenzymes in Bacteria

2011 ◽  
Vol 2011 ◽  
pp. 1-13 ◽  
Author(s):  
Meina Neumann ◽  
Silke Leimkühler
Keyword(s):  
Xanthine Oxidase ◽  
Molecular Chaperones ◽  
Molybdenum Cofactor ◽  
Complex Process ◽  
Xanthine Oxidase Family ◽  
Sulfur Ligand ◽  
Target Enzyme

Biogenesis of prokaryotic molybdoenzymes is a complex process with the final step representing the insertion of a matured molybdenum cofactor (Moco) into a folded apoenzyme. Usually, specific chaperones of the XdhC family are required for the maturation of molybdoenzymes of the xanthine oxidase family in bacteria. Enzymes of the xanthine oxidase family are characterized to contain an equatorial sulfur ligand at the molybdenum center of Moco. This sulfur ligand is inserted into Moco while bound to the XdhC-like protein and before its insertion into the target enzyme. In addition, enzymes of the xanthine oxidase family bind either the molybdopterin (Mo-MPT) form of Moco or the modified molybdopterin cytosine dinucleotide cofactor (MCD). In both cases, only the matured cofactor is inserted by a proofreading process of XdhC. The roles of these specific XdhC-like chaperones during the biogenesis of enzymes of the xanthine oxidase family in bacteria are described.

scholarly journals The role of superoxide in xanthine oxidase-induced autooxidation of linoleic acid.

1982 ◽  
Vol 257 (14) ◽  
pp. 8343-8347
Author(s):  
M J Thomas ◽  
K S Mehl ◽  
W A Pryor
Keyword(s):  
Linoleic Acid ◽  
Xanthine Oxidase

scholarly journals The Role of Molybdenum in Xanthine Oxidase and Related Enzymes

1969 ◽  
Vol 244 (10) ◽  
pp. 2658-2663 ◽  
Author(s):  
M P Coughlan ◽  
K V Rajagopalan ◽  
P Handler
Keyword(s):  
Xanthine Oxidase

Kinetics and Interactions of Molybdenum and Iron−Sulfur Centers in Bacterial Enzymes of the Xanthine Oxidase Family:  Mechanistic Implications

Biochemistry ◽  
1999 ◽  
Vol 38 (42) ◽  
pp. 14077-14087 ◽  
Author(s):  
Christoph Canne ◽  
David J. Lowe ◽  
Susanne Fetzner ◽  
Benjamin Adams ◽  
Andrew T. Smith ◽  
...  
Keyword(s):  
Xanthine Oxidase ◽  
Bacterial Enzymes ◽  
Iron Sulfur ◽  
Xanthine Oxidase Family

scholarly journals Role of Xanthine Oxidase in the Reduction of Resazurin by Raw Milk

1961 ◽  
Vol 44 (3) ◽  
pp. 425-429 ◽  
Author(s):  
J.J.R. Campbell ◽  
Lynette B. Keur
Keyword(s):  
Xanthine Oxidase ◽  
Raw Milk

Biological Role of Xanthine Oxidase and Tetrazolium-Reductase Inhibitor

1973 ◽  
Vol 33 (3) ◽  
pp. 439-445 ◽  
Author(s):  
Rainer Fried ◽  
Lygia W. Fried ◽  
Donald R. Babin
Keyword(s):  
Xanthine Oxidase ◽  
Reductase Inhibitor ◽  
Biological Role

scholarly journals The Role of Xanthine Oxidase and Xanthine Dehydrogenase in Skin Ischemia

1994 ◽  
Vol 56 (2) ◽  
pp. 162-167 ◽  
Author(s):  
Riley Rees ◽  
Del Smith ◽  
Ti Dong Li ◽  
Belinda Cashmer ◽  
Warren Garner ◽  
...  
Keyword(s):  
Xanthine Oxidase ◽  
Xanthine Dehydrogenase

Histochemical localization and possible antibacterial role of xanthine oxidase in the bovine mammary gland

1988 ◽  
Vol 55 (1) ◽  
pp. 25-32 ◽  
Author(s):  
Robert A. Collins ◽  
Keith R. Parsons ◽  
Terry R. Field ◽  
A. John Bramley
Keyword(s):  
Antibacterial Activity ◽  
Mammary Gland ◽  
Xanthine Oxidase ◽  
Histochemical Localization ◽  
Bovine Mammary Gland ◽  
Streptococcus Uberis ◽  
Antibacterial Assay ◽  
Secretory Tissue ◽  
Teat Canal

SummaryXanthine oxidase (XO) was demonstrated to be present in the teat canal and secretory tissue of the bovine mammary gland by histochemical techniques. Homogenates of these tissues were able to replace XO in an antibacterial assay with Streptococcus uberis. The action of XO on its substrate hypoxanthine was shown to provide an essential component for anti-streptococcal activity mediated by lactoperoxidase. A mechanism is proposed whereby the interaction of XO, lactoperoxidase and thiocyanate may provide antibacterial activity in the teat canal.

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