Crystallogic studies on the Complex of Carboxypeptidase A with inhibitors using alpha-hydroxy ketone as zinc-binding group

(2R)-2-benzyl-5-hydroxy-4-oxopentanoic acid

Optical 2-benzyl-5-hydroxy4oxopentanoic acids against carboxypeptidase A: Synthesis, kinetic evaluation and X-ray crystallographic study

ARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGV
WFAKKFTEDYGQDPSFTAILDSMDIFLEIVTNPDGFAFTHSQNRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSP
CSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQLLLYPYGYTTQSIPDKTELNQVAKSAVEALKSLYGTSYKY
GSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTIMEHTVNN

0.02% glutaraldehyde, 0.15M lithium chloride, pH 7.5, temperature 277K, MICRODIALYSIS

DIFFERENCE BETWEEN THE SEQRES AND THE SEQUENCE DATABASE. UNIPROT SHOWS VARIANT AT THIS POSITION.

carboxypeptidase A, alpha-hydroxy ketone, inhibitor, Carboxypeptidase, Hydrolase, Metal-binding, Metalloprotease, Polymorphism, Protease, Secreted, Zinc, Zymogen

ARSTNTFNYATYHTLDEIYDFMDLLVAEHPQLVSKLQIGRSYEGRPIYVLKFSTGGSNRPAIWIDLGIHSREWITQATGV
WFAKKFTEDYGQDPSFTAILDSMDIFLEIVTNPDGFAFTHSQNRLWRKTRSVTSSSLCVGVDANRNWDAGFGKAGASSSP
CSETYHGKYANSEVEVKSIVDFVKDHGNFKAFLSIHSYSQLLLYPYGYTTQSIPDKTELNQVAKSAVEALKSLYGTSYKY
GSIITTIYQASGGSIDWSYNQGIKYSFTFELRDTGRYGFLLPASQIIPTAQETWLGVLTIMEHTLNN