1cg2: Difference between revisions
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[[Category: metallocarboxypeptidase]] | [[Category: metallocarboxypeptidase]] | ||
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Revision as of 15:54, 30 October 2007
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CARBOXYPEPTIDASE G2
OverviewOverview
BACKGROUND: Carboxypeptidase G enzymes hydrolyze the C-terminal glutamate, moiety from folic acid and its analogues, such as methotrexate. The enzyme, studied here, carboxypeptidase G2 (CPG2), is a dimeric zinc-dependent, exopeptidase produced by Pseudomonas sp. strain RS-16. CPG2 has, applications in cancer therapy: following its administration as an, immunoconjugate, in which CPG2 is linked to an antibody to a, tumour-specific antigen, it can enzymatically convert subsequently, administered inactive prodrugs to cytotoxic drugs selectively at the, tumour site. CPG2 has no significant amino acid sequence homology with, proteins of known structure. Hence, structure determination of CPG2 was, undertaken to identify active-site residues, which may in turn provide, ideas for protein and/or ... [(full description)]
About this StructureAbout this Structure
1CG2 is a [Single protein] structure of sequence from [Pseudomonas sp.] with ZN as [ligand]. Active as [Glutamate carboxypeptidase], with EC number [3.4.17.11]. Structure known Active Sites: CTA, CTB, CTC and CTD. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy., Rowsell S, Pauptit RA, Tucker AD, Melton RG, Blow DM, Brick P, Structure. 1997 Mar 15;5(3):337-47. PMID:9083113
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