Back أكونتيز Arabic ཨེ་ཁོ་ནི་སྨིན་རྫས། Tibetan Aconitasa Catalan Akonitáza Czech Aconitase German Aconitasa Spanish Akonitaasi Finnish Aconitase French Aconitase Galician Akonitáz Hungarian
| aconitate hydratase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Illustration of pig aconitase in complex with the [Fe4S4] cluster. The protein is colored by secondary structure, and iron atoms are blue and the sulfur red.[1] | |||||||||
| Identifiers | |||||||||
| EC no. | 4.2.1.3 | ||||||||
| CAS no. | 9024-25-3 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| Aconitase family (aconitate hydratase) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of aconitase.[2] | |||||||||
| Identifiers | |||||||||
| Symbol | Aconitase | ||||||||
| Pfam | PF00330 | ||||||||
| InterPro | IPR001030 | ||||||||
| PROSITE | PDOC00423 | ||||||||
| SCOP2 | 1aco / SCOPe / SUPFAM | ||||||||
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Aconitase (aconitate hydratase; EC 4.2.1.3) is an enzyme that catalyses the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process.[3][4][5]
- ^ PDB: 7ACN; Lauble H, Kennedy MC, Beinert H, Stout CD (1992). "Crystal structures of aconitase with isocitrate and nitroisocitrate bound". Biochemistry. 31 (10): 2735–48. doi:10.1021/bi00125a014. PMID 1547214.
- ^ PDB: 1ACO; Lauble H, Kennedy MC, Beinert H, Stout CD (1994). "Crystal Structures of Aconitase with Trans-aconitate and Nitrocitrate Bound". Journal of Molecular Biology. 237 (4): 437–51. doi:10.1006/jmbi.1994.1246. PMID 8151704.
- ^ Beinert H, Kennedy MC (Dec 1993). "Aconitase, a two-faced protein: enzyme and iron regulatory factor". FASEB Journal. 7 (15): 1442–9. doi:10.1096/fasebj.7.15.8262329. PMID 8262329. S2CID 1107246.
- ^ Flint DH, Allen RM (1996). "Iron−Sulfur Proteins with Nonredox Functions". Chemical Reviews. 96 (7): 2315–34. doi:10.1021/cr950041r. PMID 11848829.
- ^ Beinert H, Kennedy MC, Stout CD (Nov 1996). "Aconitase as Ironminus signSulfur Protein, Enzyme, and Iron-Regulatory Protein". Chemical Reviews. 96 (7): 2335–2374. doi:10.1021/cr950040z. PMID 11848830.