2-methylisocitrate lyase

Details

Name
2-methylisocitrate lyase
Synonyms
  • (2R,3S)-2-methylisocitrate lyase
  • 2-MIC
  • 4.1.3.30
  • yahQ
Gene Name
prpB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0010879|2-methylisocitrate lyase
MSLHSPGKAFRAALTKENPLQIVGTINANHALLAQRAGYQAIYLSGGGVAAGSLGLPDLG
ISTLDDVLTDIRRITDVCSLPLLVDADIGFGSSAFNVARTVKSMIKAGAAGLHIEDQVGA
KRCGHRPNKAIVSKEEMVDRIRAAVDAKTDPDFVIMARTDALAVEGLDAAIERAQAYVEA
GAEMLFPEAITELAMYRQFADAVQVPILANITEFGATPLFTTDELRSAHVAMALYPLSAF
RAMNRAAEHVYNVLRQEGTQKSVIDTMQTRNELYESINYYQYEEKLDNLFARSQVK
Number of residues
296
Molecular Weight
32134.305
Theoretical pI
5.4
GO Classification
Functions
magnesium ion binding / methylisocitrate lyase activity / transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Processes
glyoxylate cycle / propionate catabolic process, 2-methylcitrate cycle
Components
cytoplasm
General Function
Transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
Specific Function
Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-carbanion intermediate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0010880|2-methylisocitrate lyase (prpB)
ATGTCTCTACACTCTCCAGGTAAAGCGTTTCGCGCTGCACTGACTAAAGAAAATCCATTG
CAGATTGTTGGCACCATCAACGCTAATCATGCGCTGTTGGCGCAGCGTGCCGGATATCAG
GCAATTTATCTTTCTGGCGGTGGCGTGGCGGCAGGTTCGCTGGGGCTGCCCGATCTCGGT
ATTTCTACCCTTGATGATGTGCTGACCGACATTCGCCGTATCACCGACGTTTGTTCGCTG
CCGCTGCTGGTGGATGCGGATATCGGTTTTGGTTCTTCGGCCTTTAACGTGGCGCGCACC
GTGAAATCGATGATTAAAGCCGGTGCGGCAGGATTGCATATTGAAGATCAGGTTGGTGCG
AAACGCTGCGGTCATCGTCCGAATAAAGCGATCGTCTCGAAAGAAGAGATGGTGGATCGG
ATCCGCGCGGCGGTGGATGCGAAAACCGATCCTGATTTTGTGATCATGGCGCGCACCGAT
GCTCTGGCGGTAGAGGGGCTGGATGCGGCGATCGAGCGTGCGCAGGCCTATGTTGAAGCG
GGTGCCGAGATGTTGTTCCCGGAGGCGATTACCGAACTCGCCATGTACCGCCAGTTTGCC
GATGCGGTGCAGGTGCCGATCCTCGCCAACATCACCGAATTTGGTGCCACGCCGCTGTTT
ACCACCGACGAATTACGCAGCGCCCATGTCGCAATGGCGCTGTACCCACTTTCAGCGTTC
CGCGCCATGAACCGCGCCGCTGAACATGTCTACAACGTCCTGCGCCAGGAAGGCACGCAG
AAAAGCGTCATCGACACCATGCAGACCCGCAACGAGCTGTACGAAAGCATCAACTACTAC
CAGTACGAAGAGAAGCTCGACAACCTGTTTGCCCGTAGCCAGGTGAAATAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP77541
UniProtKB Entry NamePRPB_ECOLI
GenBank Protein ID1657527
GenBank Gene IDU73857
General References
  1. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  2. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  3. Textor S, Wendisch VF, De Graaf AA, Muller U, Linder MI, Linder D, Buckel W: Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria. Arch Microbiol. 1997 Nov;168(5):428-36. [Article]
  4. Brock M, Darley D, Textor S, Buckel W: 2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: characterization and comparison of both enzymes. Eur J Biochem. 2001 Jun;268(12):3577-86. [Article]
  5. Grimm C, Evers A, Brock M, Maerker C, Klebe G, Buckel W, Reuter K: Crystal structure of 2-methylisocitrate lyase (PrpB) from Escherichia coli and modelling of its ligand bound active centre. J Mol Biol. 2003 May 2;328(3):609-21. [Article]
  6. Liu S, Lu Z, Han Y, Melamud E, Dunaway-Mariano D, Herzberg O: Crystal structures of 2-methylisocitrate lyase in complex with product and with isocitrate inhibitor provide insight into lyase substrate specificity, catalysis and evolution. Biochemistry. 2005 Mar 1;44(8):2949-62. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01727Isocitric AcidexperimentalunknownDetails