The DOI matches its Crossref record; 122 of the 122 references it cites were found in a registry or an index.
MOLYBDENUM COFACTOR BIOSYNTHESIS AND MOLYBDENUM ENZYMES
Abstract
The molybdenum cofactor (Moco) forms the active site of all eukaryotic molybdenum (Mo) enzymes. Moco consists of molybdenum covalently bound to two sulfur atoms of a unique tricyclic pterin moiety referred to as molybdopterin. Moco is synthesized from GTP by an ancient and conserved biosynthetic pathway that can be divided into four steps involving the biosynthetic intermediates cyclic pyranopterin monophosphate, molybdopterin, and adenylated molybdopterin. In a fifth step, sulfuration or bond formation between Mo and a protein cysteine result in two different catalytic Mo centers. There are four Mo enzymes in plants: (1) nitrate reductase catalyzes the first and rate-limiting step in nitrate assimilation and is structurally similar to the recently identified, (2) peroxisomal sulfite oxidase that detoxifies excessive sulfite. (3) Aldehyde oxidase catalyzes the last step of abscisic acid biosynthesis, and (4) xanthine dehydrogenase is essential for purine degradation and stress response.
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Cites
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840
The metabolic and molecular bases of inherited disease
Chen, Y.-T. (2001) · Medical Entomology and Zoology · Cited by 6,928
Escherichia coli and Salmonella typhimurium: Cellular and molecular biology
Lejeune, P. (1988) · Biochimie · doi:10.1016/0300-9084(88)90119-8 · Cited by 4,072
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
The Mononuclear Molybdenum Enzymes
Hille, R. (1996) · Chemical Reviews · doi:10.1021/cr950061t · Cited by 1,501
THE UBIQUITIN SYSTEM FOR PROTEIN DEGRADATION
Hershko, A., & Ciechanover, A. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.003553 · Cited by 1,410
Sofia, H. J. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.5.1097 · Cited by 1,019
Tetrahydrobiopterin biosynthesis, regeneration and functions
Thöny, B., Auerbach, G., & Blau, N. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3470001 · Cited by 893
Complex regulation of ABA biosynthesis in plants
Seo, M., & Koshiba, T. (2002) · Trends in Plant Science · doi:10.1016/s1360-1385(01)02187-2 · Cited by 795
Campbell, W. H. (1999) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.50.1.277 · Cited by 772
Cited by
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
Molybdenum cofactors, enzymes and pathways
Schwarz, G., Mendel, R. R., & Ribbe, M. W. (2009) · Nature · doi:10.1038/nature08302 · Cited by 872
Self-citationRadical S-Adenosylmethionine Enzymes
Broderick, J. B., Duffus, B. R., Duschene, K. S., & Shepard, E. M. (2014) · Chemical Reviews · doi:10.1021/cr4004709 · Cited by 830
The genomes of four tapeworm species reveal adaptations to parasitism
The Taenia solium Genome Consortium, Tsai, I. J., Zarowiecki, M., Holroyd, N., Garciarrubio, A., Sanchez-Flores, A., Brooks, K. L., Tracey, A., Bobes, R. J., Fragoso, G., et al. (2013) · Nature · doi:10.1038/nature12031 · Cited by 760
Lea, P. J., Sodek, L., Parry, M. A. J., Shewry, P. R., & Halford, N. G. (2007) · Annals of Applied Biology · doi:10.1111/j.1744-7348.2006.00104.x · Cited by 665
Metadata
- Authors
- Schwarz, G., & Mendel, R. R.
- Venue
- Annual Review of Plant Biology
- Publisher
- Annual Reviews
- Published
- 2006-06-01
- Volume
- 57
- Issue
- 1
- Pages
- 623-647
- ISSN
- 1543-5008 (ISSN-L)
- 1545-2123
- OpenAlex
- W2166125670
- Cited by
- 346
- References
- 122
- FWCI
- 1.99
- Type
- journal article
- Language
- en
- Open access
- closed
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