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Fumarate lyase

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Lyase
Identifiers
SymbolLyase_1
PfamPF00206
InterProIPR000362
PROSITEPDOC00147
SCOP21jsw / SCOPe / SUPFAM
CDDcd01362
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1yisA:13-309 1re5A:8-300 1q5nA:90-301

1dofB:88-286 1c3uB:3-286 1c3cA:3-286 1tj7B:6-301 1k62B:11-305 1aosB:20-305 1i0aA:11-305 1u15B:11-305 1u16A:11-305 1hy0A:11-305 1xwoB:11-305 1k7wA:13-307 1tjvB:13-307 1tjuA:13-307 1hy1B:13-307 1tjwA:13-307 1auwA:19-307 1jswA:13-345 1j3uB:13-342 1yfm :36-367 1kq7B:12-342 1yfeA:12-342 1fupA:12-342 1furB:12-342 2fusA:12-342 1fuqB:12-342 1fuoB:12-342

1vdkB:11-342

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.[1][2]

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.[3]
  • 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),[4] 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

[edit]
  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.
This article incorporates text from the public domain Pfam and InterPro: IPR000362