ISSN:
1432-1327
Keywords:
Key words Hydroxylase
;
Molybdenum
;
Protein crystallography
;
Pterin cofactor
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract An account of recent advances in our understanding of enzymes possessing mononuclear molybdenum active sites is presented. On the basis of a variety of structural studies, and in conjunction with comparisons among the growing number of these enzymes for which the amino acid sequences are known, it is evident that these enzymes fall into three principal families as represented by xanthine oxidase, sulfite oxidase and DMSO reductase. Structural features of the active sites of these three families are compared and contrasted, and specific mechanistic implications of the recently reported crystal structure for the aldehyde oxidoreductase from Desulfovibrio gigas are discussed.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s007750050071
