Carboxypeptidase G2
Details
- Name
- Carboxypeptidase G2
- Synonyms
- 3.4.17.11
- CPDG2
- Folate hydrolase G2
- Glutamate carboxypeptidase
- Pteroylmonoglutamic acid hydrolase G2
- Gene Name
- cpg2
- Organism
- Pseudomonas sp. (strain RS-16)
- Amino acid sequence
>lcl|BSEQ0052772|Carboxypeptidase G2 MRPSIHRTAIAAVLATAFVAGTALAQKRDNVLFQAATDEQPAVIKTLEKLVNIETGTGDA EGIAAAGNFLEAELKNLGFTVTRSKSAGLVVGDNIVGKIKGRGGKNLLLMSHMDTVYLKG ILAKAPFRVEGDKAYGPGIADDKGGNAVILHTLKLLKEYGVRDYGTITVLFNTDEEKGSF GSRDLIQEEAKLADYVLSFEPTSAGDEKLSLGTSGIAYVQVNITGKASHAGAAPELGVNA LVEASDLVLRTMNIDDKAKNLRFNWTIAKAGNVSNIIPASATLNADVRYARNEDFDAAMK TLEERAQQKKLPEADVKVIVTRGRPAFNAGEGGKKLVDKAVAYYKEAGGTLGVEERTGGG TDAAYAALSGKPVIESLGLPGFGYHSDKAEYVDISAIPRRLYMAARLIMDLGAGK
- Number of residues
- 415
- Molecular Weight
- 43931.68
- Theoretical pI
- Not Available
- GO Classification
- Functionscarboxypeptidase activity / metal ion binding / metallopeptidase activity
- General Function
- Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity.
- Specific Function
- Carboxypeptidase activity
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P06621 UniProtKB Entry Name CBPG_PSES6 - General References
- Minton NP, Atkinson T, Bruton CJ, Sherwood RF: The complete nucleotide sequence of the Pseudomonas gene coding for carboxypeptidase G2. Gene. 1984 Nov;31(1-3):31-8. doi: 10.1016/0378-1119(84)90192-6. [Article]
- Sherwood RF, Melton RG, Alwan SM, Hughes P: Purification and properties of carboxypeptidase G2 from Pseudomonas sp. strain RS-16. Use of a novel triazine dye affinity method. Eur J Biochem. 1985 May 2;148(3):447-53. doi: 10.1111/j.1432-1033.1985.tb08860.x. [Article]
- Rowsell S, Pauptit RA, Tucker AD, Melton RG, Blow DM, Brick P: Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy. Structure. 1997 Mar 15;5(3):337-47. doi: 10.1016/s0969-2126(97)00191-3. [Article]