Hydrolysis of S-2-aminoethylcysteinyl peptide bond by Achromobacter protease I.
The substrate specificity of Achromobacter protease I (API) was examined for S-2-aminoethyl(AE)cysteinyl bonds in Bz-AEC-OMe/OEt, Bz-AEC-NH2, and AE-insulin B chain. The protease hydrolyzed all of the tested AE-cysteinyl bonds at the same rate as that of lysyl bonds. Kinetic parameters were estimated for this hydrolysis reaction.
Masaki
T
T
Department of Resource Biology, Faculty of Agriculture, Ibaraki University, Japan.
Takiya
T
T
Tsunasawa
S
S
Kuwahara
S
S
Sakiyama
F
F
Soejima
M
M
D000421:Alcaligenes / Q000201:enzymology*; D000595:Amino Acid Sequence; D003545:Cysteine / Q000031:analogs & derivatives* / Q000378:metabolism; D010450:Endopeptidases / Q000378:metabolism*; D006868:Hydrolysis; D007328:Insulin / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D010455:Peptides / Q000378:metabolism*
D007328:Insulin; D010455:Peptides; C000204:S-2-aminoethyl cysteine; D010450:Endopeptidases; D003545:Cysteine