6-oxocamphor hydrolase

Details

Name
6-oxocamphor hydrolase
Synonyms
  • 3.7.1.18
  • Beta-diketone hydrolase
  • OCH
Gene Name
camK
Organism
Rhodococcus sp.
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
Functions
hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
General Function
Hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances
Specific 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.
Pfam Domain Function
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
ResourceLink
UniProtKB IDQ93TU6
UniProtKB Entry NameCAMK_RHOSO
GenBank Gene IDAF323755
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02906(2s,4s)-Alpha-Campholinic AcidexperimentalunknownDetails