6-oxocamphor hydrolase
Details
- Name
- 6-oxocamphor hydrolase
- Kind
- protein
- Synonyms
- 3.7.1.18
- Beta-diketone hydrolase
- OCH
- Gene Name
- camK
- UniProtKB Entry
- Q93TU6Swiss-Prot
- Organism
- Rhodococcus sp.
- NCBI Taxonomy ID
- 1831
- Amino acid sequence
>lcl|BSEQ0022042|6-oxocamphor hydrolase MKQLATPFQEYSQKYENIRLERDGGVLLVTVHTEGKSLVWTSTAHDELAYCFHDIACDRE NKVVILTGTGPSFCNEIDFTSFNLGTPHDWDEIIFEGQRLLNNLLSIEVPVIAAVNGPVT NHPEIPVMSDIVLAAESATFQDGPHFPSGIVPGDGAHVVWPHVLGSNRGRYFLLTGQELD ARTALDYGAVNEVLSEQELLPRAWELARGIAEKPLLARRYARKVLTRQLRRVMEADLSLG LAHEALAAIDLGMESEQ
- Number of residues
- 257
- Molecular Weight
- 28483.03
- Theoretical pI
- 4.72
- GO Classification
- Functionshydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
- General Function
- Catalyzes the carbon-carbon bond cleavage of the bicyclic beta-diketone 6-oxocamphor via a retro-Claisen reaction to yield the optically active (2R,4S)-beta-campholinic acid. It is also able to cleave 2,2-disubstituted cyclohexa-1,3-diones such as 2-methyl-2-propylcyclohexa-1,3-dione and 2-methyl-2-butylcyclohexa-1,3-dione which result in racemic keto acid products. Transformations of the bicyclic diketone substrates bicyclo[2.2.1]heptane 2,6-dione and bicyclo[2.2.2]octane-2,6-dione yield (S)-keto acid products.
- Specific Function
- hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
- Pfam Domain Function
- ECH_1 (PF00378)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0005570|774 bp ATGAAGCAATTGGCCACCCCCTTCCAGGAGTACTCACAGAAGTACGAGAACATCCGCCTC GAACGAGACGGCGGCGTCCTCCTGGTCACCGTCCACACCGAAGGCAAGAGCCTGGTGTGG ACCTCAACCGCACACGACGAGCTGGCCTACTGCTTCCACGACATCGCGTGCGACCGGGAG AACAAGGTCGTCATCCTCACCGGCACCGGCCCCTCGTTCTGCAACGAGATCGACTTCACC TCGTTCAACCTCGGCACCCCGCACGACTGGGACGAGATCATCTTCGAAGGCCAGCGTCTG CTCAACAACCTGCTGAGTATCGAGGTGCCGGTCATCGCGGCGGTCAACGGACCGGTGACC AACCACCCGGAGATCCCCGTCATGTCGGACATCGTCCTCGCCGCGGAGTCCGCCACCTTC CAGGACGGACCGCACTTCCCTTCCGGCATCGTGCCCGGGGACGGCGCCCACGTGGTGTGG CCGCACGTGCTGGGCTCGAACCGTGGACGCTACTTCCTGCTGACCGGCCAGGAACTCGAT GCTCGCACCGCCCTCGACTACGGCGCGGTCAACGAGGTCCTGTCCGAGCAGGAGCTGCTG CCCCGCGCCTGGGAGCTCGCCCGCGGTATCGCCGAGAAACCGCTCCTGGCCCGCCGGTAC GCCCGCAAGGTGCTGACCCGTCAGCTGCGGCGGGTCATGGAAGCCGACCTGAGTCTCGGC CTCGCGCACGAAGCGCTCGCCGCCATCGATCTGGGAATGGAGTCCGAACAGTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID Q93TU6 UniProtKB Entry Name CAMK_RHOSO GenBank Gene ID AF323755 PDB ID(s) 1O8U, 1SZO KEGG ID ag:AAK50622 - General References
- Grogan G, Roberts GA, Bougioukou D, Turner NJ, Flitsch SL: The desymmetrization of bicyclic beta -diketones by an enzymatic retro-Claisen reaction. A new reaction of the crotonase superfamily. J Biol Chem. 2001 Apr 20;276(16):12565-72. Epub 2001 Jan 16. [Article]
- Roberts GA, Grogan G, Turner NJ, Flitsch SL: Nucleotide sequence of a portion of the camphor-degrading gene cluster from Rhodococcus sp. NCIMB 9784. DNA Seq. 2004 Apr;15(2):96-103. [Article]
- Whittingham JL, Turkenburg JP, Verma CS, Walsh MA, Grogan G: The 2-A crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily. J Biol Chem. 2003 Jan 17;278(3):1744-50. Epub 2002 Nov 5. [Article]
- Leonard PM, Grogan G: Structure of 6-oxo camphor hydrolase H122A mutant bound to its natural product, (2S,4S)-alpha-campholinic acid: mutant structure suggests an atypical mode of transition state binding for a crotonase homolog. J Biol Chem. 2004 Jul 23;279(30):31312-7. Epub 2004 May 11. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details (2s,4s)-Alpha-Campholinic Acid experimental unknown target Details