Global InformationMaleate isomerase information
| Maleate Isomerase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Maleate isomerase from Pseudomonas putida | |||||||||
| Identifiers | |||||||||
| EC no. | 5.2.1.1 | ||||||||
| CAS no. | 9023-74-9 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a maleate isomerase (EC 5.2.1.1), or maleate cis-tran isomerase, is a member of the Asp/Glu racemase superfamily discovered in bacteria. It is responsible for catalyzing cis-trans isomerization of the C2-C3 double bond in maleate to produce fumarate,[1] which is a critical intermediate in citric acid cycle.[2] The presence of an exogenous mercaptan is required for catalysis to happen.[3]
Illustration of the overall isomerization catalyzed by maleate isomerase
Maleate isomerase participates in butanoate metabolism and nicotinate and nicotinamide metabolism.[4] It is an essential enzyme for the last step of metabolic degradation pathway of nicotinic acid. Recently, maleate isomerase has been an industrial target for degradation of tobacco waste.[5][6] It is also got attention for its involvement in aspartic acid and maleic acid production.[7][8][9]
Maleate isomerase has been utilized by multiple bacteria species, including Pseudomonas fluorescens,[3] Alcaligenes faecalis,[10] Bacillus stearothermophilus,[11] Serratia marcescens[8], Pseudomonas putida[12] and Nocardia farcinica.[1][5] The enzyme has a molecular weight of 74,000 and a turnover number of 1,800 moles per mole of protein per min.[3]
- ^ a b Fisch F, Fleites CM, Delenne M, Baudendistel N, Hauer B, Turkenburg JP, Hart S, Bruce NC, Grogan G (August 2010). "A covalent succinylcysteine-like intermediate in the enzyme-catalyzed transformation of maleate to fumarate by maleate isomerase". Journal of the American Chemical Society. 132 (33): 11455–7. doi:10.1021/ja1053576. PMID 20677745.
- ^ Tanaka K, Kobayashi K, Ogasawara N (September 2003). "The Bacillus subtilis YufLM two-component system regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium". Microbiology. 149 (Pt 9): 2317–29. doi:10.1099/mic.0.26257-0. PMID 12949159.
- ^ a b c Scher W, Jakoby WB (April 1969). "Maleate isomerase". The Journal of Biological Chemistry. 244 (7): 1878–82. doi:10.1016/S0021-9258(18)91762-X. PMID 5780844.
- ^ Behrman EJ, Stanier RY (October 1957). "The bacterial oxidation of nicotinic acid". The Journal of Biological Chemistry. 228 (2): 923–45. doi:10.1016/S0021-9258(18)70671-6. PMID 13475371.
- ^ a b Chen D, Tang H, Lv Y, Zhang Z, Shen K, Lin K, Zhao YL, Wu G, Xu P (March 2013). "Structural and computational studies of the maleate isomerase from Pseudomonas putida S16 reveal a breathing motion wrapping the substrate inside". Molecular Microbiology. 87 (6): 1237–44. doi:10.1111/mmi.12163. PMID 23347155. S2CID 13313674.
- ^ Tang H, Yao Y, Wang L, Yu H, Ren Y, Wu G, Xu P (2012). "Genomic analysis of Pseudomonas putida: genes in a genome island are crucial for nicotine degradation". Scientific Reports. 2: 377. doi:10.1038/srep00377. PMC 3332521. PMID 22530095.
- ^ Roa Engel CA, Straathof AJ, Zijlmans TW, van Gulik WM, van der Wielen LA (March 2008). "Fumaric acid production by fermentation". Applied Microbiology and Biotechnology. 78 (3): 379–89. doi:10.1007/s00253-007-1341-x. PMC 2243254. PMID 18214471.
- ^ a b Hatakeyama K, Goto M, Kobayashi M, Terasawa M, Yukawa H (July 2000). "Analysis of oxidation sensitivity of maleate cis-trans isomerase from Serratia marcescens". Bioscience, Biotechnology, and Biochemistry. 64 (7): 1477–85. doi:10.1271/bbb.64.1477. PMID 10945267.
- ^ Dokainish HM, Ion BF, Gauld JW (June 2014). "Computational investigations on the catalytic mechanism of maleate isomerase: the role of the active site cysteine residues". Physical Chemistry Chemical Physics. 16 (24): 12462–74. doi:10.1039/c4cp01342e. PMID 24827730.
- ^ Hatakeyama K, Asai Y, Uchida Y, Kobayashi M, Terasawa M, Yukawa H (October 1997). "Gene cloning and characterization of maleate cis-trans isomerase from Alcaligenes faecalis". Biochemical and Biophysical Research Communications. 239 (1): 74–9. doi:10.1006/bbrc.1997.7430. PMID 9345272.
- ^ Hatakeyama K, Goto M, Uchida Y, Kobayashi M, Terasawa M, Yukawa H (March 2000). "Molecular analysis of maleate cis-trans isomerase from thermophilic bacteria". Bioscience, Biotechnology, and Biochemistry. 64 (3): 569–76. doi:10.1271/bbb.64.569. PMID 10803955. S2CID 43798064.
- ^ Jiménez JI, Canales A, Jiménez-Barbero J, Ginalski K, Rychlewski L, García JL, Díaz E (August 2008). "Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440". Proceedings of the National Academy of Sciences of the United States of America. 105 (32): 11329–34. doi:10.1073/pnas.0802273105. PMC 2516282. PMID 18678916.