EFFECT OF ARGININE-48 REPLACEMENT ON THE REACTION BETWEEN CYTOCHROME C PEROXIDASE AND HYDROGEN PEROXIDE

X-Ray Structures of Recombinant Yeast Cytochrome C Peroxidase and Three Heme Cleft Mutants Prepared by Site-Directed Mutagenesis

Crystal Structure of Yeast Cytochrome C Peroxidase Refined at 1.7 Angstroms Resolution

MITTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVLLAWHISGTWDKHDNTGGSYGGTYRFKKEFN
DPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGYVRTFF
QRLNMNDREVVALMGAHALGKTHLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSL
IQDPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL

ACTIVE SITE WATER MOLECULE HOH-595 HAD VERY LOW OCCUPANCY IN THE R48L MUTANT, AND WAS NOT INCLUDED IN THE MODEL.

THE SEQUENCE DIFFERS FROM THAT REPORTED FOR 2CYP AT RESIDUE
272. IN THE PRESENT ENTRY, THIS RESIDUE IS REPORTED AS
ASN. THIS CORRECTS AN ERROR INTRODUCED IN 2CYP, WHERE THE
RESIDUE IS INCORRECTLY REPORTED TO BE ASP.

RESIDUES ARE NUMBERED TO BE CONSISTENT WITH THE SEQUENCE OF
THE NATIVE (2CYP) STRUCTURE. THUS THE FIRST TWO RESIDUES
HAVE RESIDUE NUMBERS -1 AND 0, RESPECTIVELY.

MTTAVRLLPSLGRTAHKRSLYLFSAAAAAAAAATFAYSQSQKRSSSSPGGGSNHGWNNWGKAAALASTTPLVHVASVEKG
RSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHTSGTWDKHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLE
PIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMG
AHALGKTHLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSIVKEYAN
DQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL