Disease relevance of CCP1

• No role for CCP1 was apparent in cells exposed to heat stress under aerobic or anaerobic conditions [1].
• By use of site-directed mutagenesis and an Escherichia coli expression system, a mutant phenylalanine-191 (F191) CCP was prepared in order to examine the effects of altering the H-bonding and pi-pi interactions that occur between Trp-191 and the iron-coordinated proximal His-175 in the parent enzyme [2].
• Only the subjects treated with CPO/SA shampoo showed a significant reduction in the itching of seborrhoeic dermatitis at these times [3].
• CCP 25 also inhibited translation of brome mosaic virus (BMV) and pokeweed mosaic virus (PMV) RNAs in rabbit reticulocyte translation system [4].

High impact information on CCP1

• Mutant proteins containing Leu, Arg, Met, or Pro at residue 175 of mature CCP were sensitive to proteolysis and were imported into isolated mitochondria as judged by proteolytic processing of the precursor [5].
• UV-visible spectroscopic and stopped-flow studies indicate that CCP in the covalent complex reacts normally with H(2)O(2) to give compound I [6].
• Transient kinetics were examined for the oxidation of eight mono-substituted anilines by CCP, W51F, and W51A [7].
• Each of the aniline derivatives were oxidized by the mutants at rates that exceeded that of the wild-type enzyme, and the rate constant for m-chloroaniline was 400-fold faster for W51F than for wild-type CCP [7].
• Using site-directed mutagenesis, a double mutant in yeast cytochrome c peroxidase (CCP) has been constructed where the proximal ligand, His175, has been converted to glutamine and the neighboring Trp191 has been converted to phenylalanine [8].

Chemical compound and disease context of CCP1

• In particular, we have examined the ferric states of yeast wild-type CCP (YCCP), CCP (MKT) which is the form of the enzyme that is expressed in and purified from E. coli, and contains Met-Lys-Thr (MKT) at the N-terminus, CCP (MKT) in the presence of 60% glycerol, lyophilized YCCP, and alkaline CCP (MKT) [9].
• CONCLUSION: The study demonstrated that both CPO/SA and Nizoral were safe and effective in the treatment of dandruff and seborrhoeic dermatitis [3].

Biological context of CCP1

• In this study, the complex, oxidative responsive, CCP1 promoter was used as a model to investigate the cis-acting elements responsible for activation by oxidative stress [10].
• A null allele of yeast CCP1 gene encoding CcP was created by one-step gene disruption method in a diploid yeast strain [11].
• Haploid yeast cells with the disrupted CCP1 gene were viable and able to grow in a medium containing lactic acid or glycerol as an energy source, indicating that CcP is not essential for both cell viability and respiration [11].
• The results suggest that, in addition to stabilizing the reactive intermediate compound I, the distal arginine plays an important role as a gatekeeper in the active site of CCP, controlling the access to the ferryl oxygen and the distal histidine [12].
• Cytochrome c peroxidase (CCP) from Saccharomyces cerevisiae was subjected to directed molecular evolution to generate mutants with increased activity against the classical peroxidase substrate guaiacol, thus changing the substrate specificity of CCP from the protein cytochrome c to a small organic molecule [12].

Anatomical context of CCP1

• Ribosomal RNA yielded 360 nucleotide base fragment after treatment with CCP 25 indicating that CCP 25 was a ribosome inactivating protein [4].

Associations of CCP1 with chemical compounds

• Moreover, expression of CCP1 gene increased by treatments with peroxynitrite, indicating that CcP may act as a peroxynitrite scavenger [11].
• CCP1-null-mutant cells in the W303-1B genetic background (ccp1Delta) grew as well as wild-type cells with glucose, ethanol, glycerol or lactate as carbon sources but with a shorter initial doubling time [1].
• Cytochrome c peroxidase (CCP) is a 32.5 kDa mitochondrial intermembrane space heme peroxidase from Saccharomyces cerevisiae that reduces H(2)O(2) to 2H(2)O by oxidizing two molecules of cytochrome c (cyt c) [13].
• The role of tryptophan residues as endogenous electron donors in cytochrome c peroxidase (CCP) was examined by protein steady-state fluorescence [14].
• Here we compare the 1.2 A native structure (CCP) with the 1.3 A structure of its stable oxidized reaction intermediate, Compound I (CCP1) [13].

Analytical, diagnostic and therapeutic context of CCP1

• To test whether premature heme addition to the apoprecursor was responsible for the protease resistance and the inability to import preCCP, site-directed mutagenesis was used to replace the axial heme ligand (His175) involved in forming a pseudo-covalent link between the heme iron and CCP [5].
• Following myoglobin and CCP incubation with a 10-fold molar excess of H(2)O(2) and TEMPO(*), matrix-assisted laser desorption ionization (MALDI) time-of-flight analysis of the tryptic peptides derived from the proteins revealed 1 and 9 TEMPO adducts of myoglobin and CCP, respectively [15].
• Transient resonance Raman, Raman difference, circular dichroism (CD), and optical absorption studies have been carried out on the electrostatic complexes formed by yeast cytochrome c peroxidase (CCP) with horse cytochrome c (Cytc) in low ionic strength solutions [16].
• Complex formation between ferricytochrome c peroxidase (CCP) and ferricytochrome c from yeast [cyt(Y)] and horse heart [cyt(H)] was studied by resonance Raman spectroscopy [17].
• X-ray crystallography showed that a5Ru is coordinated to His60 in one derivative [Fox et al. (1990) J. Am. Chem. Soc. 112, 7426]; HPLC and mass spectral analysis of the tryptic peptides of the other derivative identified a peptide (MW = 1469 Da) corresponding to residues 1-12 of CCP plus a5Ru, indicating His6 as the site of modification [18].

References