Identification |
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Name: | 4-hydroxy-2-oxovalerate aldolase |
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Synonyms: | - HOA
- 4-hydroxy-2-keto-pentanoic acid aldolase
- 4-hydroxy-2-oxopentanoate aldolase
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Gene Name: | mhpE |
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Enzyme Class: | |
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Biological Properties |
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General Function: | Involved in 4-hydroxy-2-oxovalerate aldolase activity |
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Specific Function: | Catalyzes the retro-aldol cleavage of 4-hydroxy-2- oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of 3-phenylpropanoate |
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Cellular Location: | Not Available |
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SMPDB Pathways: | |
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KEGG Pathways: | |
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KEGG Reactions: | |
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SMPDB Reactions: | |
1.04-hydroxy-2-oxopentanoate | + | 1.0 | → | 1.0 | + | 1.0 |
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EcoCyc Reactions: | |
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Metabolites: | |
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GO Classification: | Function |
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4-hydroxy-2-oxovalerate aldolase activity | carbon-carbon lyase activity | catalytic activity | lyase activity | oxo-acid-lyase activity | Process |
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aromatic compound catabolic process | cellular aromatic compound metabolic process | cellular metabolic process | metabolic process |
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Gene Properties |
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Blattner: | b0352 |
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Gene Orientation | Clockwise |
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Centisome Percentage: | 8.04 |
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Left Sequence End | 373092 |
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Right Sequence End | 374105 |
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Gene Sequence: | >1014 bp
ATGAACGGTAAAAAACTTTATATCTCGGACGTCACATTGCGTGACGGTATGCACGCCATT
CGTCATCAGTATTCGCTGGAAAACGTTCGCCAGATTGCCAAAGCACTGGACGATGCCCGC
GTGGATTCGATTGAAGTGGCCCACGGCGACGGTTTGCAAGGTTCCAGCTTTAACTATGGT
TTCGGCGCACATAGCGACCTTGAATGGATTGAAGCGGCGGCGGATGTGGTGAAGCACGCC
AAAATCGCGACGTTGTTGCTGCCAGGAATCGGCACTATTCACGATCTGAAAAATGCCTGG
CAGGCTGGCGCGCGGGTGGTTCGTGTGGCAACGCACTGTACCGAAGCTGATGTTTCCGCC
CAGCATATTCAGTATGCCCGCGAGCTCGGAATGGACACCGTTGGTTTTCTGATGATGAGC
CATATGACCACGCCGGAGAATCTCGCCAAGCAGGCAAAGCTGATGGAAGGCTACGGTGCG
ACCTGTATTTATGTGGTGGATTCTGGCGGTGCGATGAACATGAGCGATATCCGTGACCGT
TTCCGCGCCCTGAAAGCAGAGCTGAAACCAGAAACGCAAACTGGCATGCACGCTCACCAT
AACCTGAGTCTTGGCGTGGCGAACTCTATCGCGGCGGTGGAAGAGGGCTGCGACCGAATC
GACGCCAGCCTCGCGGGAATGGGCGCGGGCGCAGGTAACGCACCGCTGGAAGTGTTTATT
GCCGCCGCGGATAAACTGGGCTGGCAGCATGGGACCGATCTCTATGCGTTAATGGATGCC
GCCGACGACCTGGTGCGTCCGTTGCAGGATCGACCGGTACGAGTCGATCGCGAAACGCTG
GCGCTGGGATACGCTGGTGTTTACTCGAGCTTCCTGCGTCACTGTGAAACGGCGGCGGCG
CGTTATGGCTTAAGTGCGGTGGATATTCTCGTTGAGCTGGGCAAACGCCGGATGGTTGGC
GGCCAGGAGGATATGATCGTTGACGTGGCGCTGGATCTGCGCAACAACAAATAA |
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Protein Properties |
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Pfam Domain Function: | |
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Protein Residues: | 337 |
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Protein Molecular Weight: | 36470 |
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Protein Theoretical pI: | 6 |
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Signaling Regions: | |
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Transmembrane Regions: | |
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Protein Sequence: | >4-hydroxy-2-oxovalerate aldolase
MNGKKLYISDVTLRDGMHAIRHQYSLENVRQIAKALDDARVDSIEVAHGDGLQGSSFNYG
FGAHSDLEWIEAAADVVKHAKIATLLLPGIGTIHDLKNAWQAGARVVRVATHCTEADVSA
QHIQYARELGMDTVGFLMMSHMTTPENLAKQAKLMEGYGATCIYVVDSGGAMNMSDIRDR
FRALKAELKPETQTGMHAHHNLSLGVANSIAAVEEGCDRIDASLAGMGAGAGNAPLEVFI
AAADKLGWQHGTDLYALMDAADDLVRPLQDRPVRVDRETLALGYAGVYSSFLRHCETAAA
RYGLSAVDILVELGKRRMVGGQEDMIVDVALDLRNNK |
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References |
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External Links: | |
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General Reference: | - Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
- Lee, S. J., Ko, J. H., Kang, H. Y., Lee, Y. (2006). "Coupled expression of MhpE aldolase and MhpF dehydrogenase in Escherichia coli." Biochem Biophys Res Commun 346:1009-1015. Pubmed: 16782065
- Pollard, J. R., Rialland, D., Bugg, T. D. (1998). "Substrate selectivity and biochemical properties of 4-hydroxy-2-keto-pentanoic acid aldolase from Escherichia coli." Appl Environ Microbiol 64:4093-4094. Pubmed: 9758851
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