A structural comparison of molybdenum cofactor-containing enzymes

• Published in: FEMS microbiology reviews Vol. 22; no. 5; pp. 503 - 521
• Main Authors: Kisker, Caroline, Schindelin, Hermann, Baas, Dietmar, Rétey, Janos, Meckenstock, Rainer U., Kroneck, Peter M.H.
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.12.1998; Oxford University Press
• Subjects: Acetylene; Acetylene hydratase; Amino acid sequence; Amino acids; Bacteria, Anaerobic - enzymology; Coenzymes - chemistry; Enzymes; Humans; Hydro-Lyases - chemistry; Iron–sulfur cluster; Metalloproteins - chemistry; Mixed Function Oxygenases - chemistry; Molybdenum; Molybdenum enzymes; Molybdo‐pterin; Oxidoreductases - chemistry; Oxidoreductases Acting on Sulfur Group Donors - chemistry; Phloroglucinol; Pteridines - chemistry; Pyrogallol; Reductase; Reductases; Stoichiometry; Structure-function relationships; Transhydroxylase; Tungsten; Tungsten - chemistry; Tungsten enzymes; Xanthine Oxidase - chemistry; Molybdo-pterin; Transhydroxylase; Acetylene hydratase; Molybdenum enzymes; Tungsten enzymes; Iron–sulfur cluster
• ISSN: 0168-6445; 1574-6976; 1574-6976
• DOI: 10.1111/j.1574-6976.1998.tb00384.x

Abstract This work gives an overview of the recent achievements which have contributed to the understanding of the structure and function of molybdenum and tungsten enzymes. Known structures of molybdo-pterin cofactor-containing enzymes will be described briefly and the structural differences between representatives of the same and different families will be analyzed. This comparison will show that the molybdo-pterin cofactor-containing enzymes represent a very heterogeneous group with differences in overall enzyme structure, cofactor composition and stoichiometry, as well as differences in the immediate molybdenum environment. Two recently discovered molybdo-pterin cofactor-containing enzymes will be described with regard to molecular and EPR spectroscopic properties, pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici and acetylene hydratase from Pelobacter acetylenicus. On the basis of its amino acid sequence, transhydroxylase can be classified as a member of the dimethylsulfoxide reductase family, whereas classification of the tungsten/molybdenum-containing acetylene hydratase has to await the determination of its amino acid sequence.