Misplaced Pages

This article has multiple issues. Please help improve it or discuss these issues on the talk page. (Learn how and when to remove these messages) This article is an orphan, as no other articles link to it. Please introduce links to this page from related articles; try the Find link tool for suggestions. (October 2020) This article's use of external links may not follow Misplaced Pages's policies or guidelines. Please improve this article by removing excessive or inappropriate external links, and converting useful links where appropriate into footnote references. (November 2020) (Learn how and when to remove this message) (Learn how and when to remove this message)

Fumarate lyase belongs to the lyase class of enzymes. These proteins use fumarate as a substrate. They have been shown to share a short conserved sequence around a methionine which is probably involved in the catalytic activity of this type of enzymes.

The following are examples of members of this family:

• 3-carboxymuconate lactonizing enzyme, EC 5.5.1.2 (3-carboxy-cis,cis-muconate cycloisomerase), an enzyme involved in aromatic acids catabolism.
• Delta-crystallin shares around 90% sequence identity with arginosuccinate lyase, showing that it is an example of a 'hijacked' enzyme - accumulated mutations have, however, rendered the protein enzymatically inactive.
• Class I Fumarase enzyme, EC 4.2.1.2 (fumarate hydratase), which catalyzes the reversible hydration of fumarate to L-malate. Class I enzymes are thermolabile dimeric enzymes (as for example: Escherichia coli fumA and fumB).
• Arginosuccinase, EC 4.3.2.1 (argininosuccinate lyase), which catalyzes the formation of arginine and fumarate from argininosuccinate, the last step in the biosynthesis of arginine.
• Aspartate ammonia-lyase, EC 4.3.1.1 (aspartase), which catalyzes the reversible conversion of aspartate to fumarate and ammonia. This reaction is analogous to that catalyzed by fumarase, except that ammonia rather than water is involved in the trans-elimination reaction.
• class II Fumarase enzyme, EC 4.2.1.2, are thermostable and tetrameric and are found in prokaryotes (as for example: Escherichia coli fumC) as well as in eukaryotes. The sequence of the two classes of fumarases are not closely related.
• Adenylosuccinase, EC 4.3.2.2 (adenylosuccinate lyase), which catalyzes the eighth step in the de novo biosynthesis of purines, the formation of 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide and fumarate from 1-(5- phosphoribosyl)-4-(N-succino-carboxamide). That enzyme can also catalyze the formation of fumarate and AMP from adenylosuccinate.

References

1. Guest JR, Woods SA, Schwartzbach SD (1988). "Two biochemically distinct classes of fumarase in Escherichia coli". Biochim. Biophys. Acta. 954 (1): 14–26. doi:10.1016/0167-4838(88)90050-7. PMID 3282546.
2. Guest JR, Woods SA, Miles JS (1988). "Sequence homologies between arginosuccinase, aspartase and fumarase - a family of strycturally related enzymes". FEMS Microbiol. Lett. 51 (2–3): 181–186. doi:10.1111/j.1574-6968.1988.tb02994.x.
3. Babbitt PC, Ransom SC, Williams SE, Woolridge EM, Landro JA, Kozarich JW (1992). "3-Carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida is homologous to the class II fumarase family: a new reaction in the evolution of a mechanistic motif". Biochemistry. 31 (40): 9768–9776. doi:10.1021/bi00155a033. PMID 1390752.
4. Dixon JE, Zalkin H (1992). "De novo purine nucleotide biosynthesis". Prog. Nucleic Acid Res. Mol. Biol. Progress in Nucleic Acid Research and Molecular Biology. 42: 259–287. doi:10.1016/s0079-6603(08)60578-4. ISBN 9780125400428. PMID 1574589.

• v
• t
• e

• Protein domains
• Lyases
• Lyase stubs