PRX2A_COPCI
  Name and origin · Biochemical properties · Enzyme annotation · Literature · Protein features · Sequences · Cross-refs · Entry history
Name and origin
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Gene Name
Name: prx2A
Other given name: CiP
Protein names
Common name: peroxidase
EC systematic name: phenolic donor:hydrogen-peroxide oxidoreductase
Other name:
Organism
Species: Coprinopsis cinerea
Strain: IFO 30114
Taxonomic identifier: 5346
Taxonomic lineage: Eukaryota › Fungi › Dikarya › Basidiomycota › Agaricomycotina › Homobasidiomycetes › Agaricomycetidae › Agaricales › Psathyrellaceae › Coprinopsis
Enzyme activity
Biochemical properties
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General properties
Expression host
Substrate
Assay
Temperature Optimum(°C)
Temperature Stability(°C)
pH Optimum
pH Stability
Kinetic properties
Host Substrate Activity assay conditions Specific activity Relative activity(%) Assay Reference
Activity assay
native 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonate) and 4-aminoantipyrine mixture 0.5M phosphate buffer, pH 7.0, 10mM hydrogen peroxide, 550nm. active spectrophotometric assay.
 
Host Substrate Activity assay conditions Product formed Product analysis Reference
Product analysis
 
Host Substrate Kinetic assay conditions Km Kcat(s-1) Vmax Reference
Kinetic assay
 
Other features
- The minor band visualized by SDS-PAGE was explained by the fact that 20% of the enzyme sample was found to have a "nick" where the C-terminal segment appeared to be linked to the rest of the molecule by a disulfide bridge.
- Contains a heme prosthetic group.
Enzyme annotation
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Enzyme
   Enzyme commission
1.11.1.7; phenolic donor:hydrogen-peroxide oxidoreductase
Gene Ontology
GO ID Term Evidence Reference
   Biological process
GO:0055114 oxidation-reduction process IDA
GO:0042744 hydrogen peroxide catabolic process IDA
   Molecular function
GO:0004601 peroxidase activity IDA
   Cellular component
GO:0005576 extracellular region IDA
Literature
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[1] Comparison of structure and activities of peroxidases from Coprinus cinereus, Coprinus macrorhizus and Arthromyces ramosus.  
Author Kjalke M, Andersen MB, Schneider P, Christensen B, Schülein M and Welinder KG
Journal Biochim. Biophys. Acta 1992 Apr 17;1120(3):248-56.
Address Institute of Biochemical Genetics, University of Copenhagen, Denmark.
Abstract Initial structural and kinetic data suggested that peroxidases from Coprinus cinereus, Coprinus macrorhizus and Arthromyces ramosus were similar. Therefore they were characterized more fully. The three peroxidases were purified to RZ 2.5 and showed immunochemical identity as well as an identical M(r) of 38,000, pI about 3.5 and similar amino acid compositions. The N-termini were blocked for amino acid sequencing. The peroxidases had similar retention volumes by anion-exchange and gel-filtration chromatography. All peroxidases showed multiple peaks by Concanavalin A-Sepharose chromatography. The Concanavalin A-Sepharose profiles were different and depended furthermore on a fermentation batch. Tryptic peptide maps were very similar except for one peptide. This peptide contained an N-linked glycan composed of varying ratios of glucosamine and mannose for the three peroxidases. Rate constants and their pH dependence were the same for the three peroxidases using guaiacol or iodide as reducing substrates. We conclude that peroxidases from Coprinus cinereus, Coprinus macrorhizus and Arthromyces ramosus are most likely identical in their amino acid sequences, but deviate in glycosylation which, apparently, has no influence on the reaction rates of the enzyme. We suggest, that the Coprinus fungi express one peroxidase only in contrast to the lignin-degrading white-rot Basidiomycetes, which produce multiple peroxidase isozymes.
[3] Amino acid sequence of Coprinus macrorhizus peroxidase and cDNA sequence encoding Coprinus cinereus peroxidase. A new family of fungal peroxidases.  
Author Baunsgaard L, Dalbøge H, Houen G, Rasmussen EM and Welinder KG
Journal Eur. J. Biochem. 1993 Apr 1;213(1):605-11.
Address Institute of Biochemical Genetics, University of Copenhagen, Denmark.
Abstract Sequence analysis and cDNA cloning of Coprinus peroxidase (CIP) were undertaken to expand the understanding of the relationships of structure, function and molecular genetics of the secretory heme peroxidases from fungi and plants. Amino acid sequencing of Coprinus macrorhizus peroxidase, and cDNA sequencing of Coprinus cinereus peroxidase showed that the mature proteins are identical in amino acid sequence, 343 residues in size and preceded by a 20-residue signal peptide. Their likely identity to peroxidase from Arthromyces ramosus is discussed. CIP has an 8-residue, glycine-rich N-terminal extension blocked with a pyroglutamate residue which is absent in other fungal peroxidases. The presence of pyroglutamate, formed by cyclization of glutamine, and the finding of a minor fraction of a variant form lacking the N-terminal residue, indicate that signal peptidase cleavage is followed by further enzymic processing. CIP is 40-45% identical in amino-acid sequence to 11 lignin peroxidases from four fungal species, and 42-43% identical to the two known Mn-peroxidases. Like these white-rot fungal peroxidases, CIP has an additional segment of approximately 40 residues at the C-terminus which is absent in plant peroxidases. Although CIP is much more similar to horseradish peroxidase (HRP C) in substrate specificity, specific activity and pH optimum than to white-rot fungal peroxidases, the sequences of CIP and HRP C showed only 18% identity. Hence, CIP qualifies as the first member of a new family of fungal peroxidases. The nine invariant residues present in all plant, fungal and bacterial heme peroxidases are also found in CIP. The present data support the hypothesis that only one chromosomal CIP gene exists. In contrast, a large number of secretory plant and fungal peroxidases are expressed from several peroxidase gene clusters. Analyses of three batches of CIP protein and of 49 CIP clones revealed the existence of only two highly similar alleles indicating less peroxidase polymorphism in C. cinereus strains than observed in plants and white-rot fungi.
Protein features
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Signal Peptide (Predicted) SP(18aa)
N-Terminal (Experimental)
Structure PMID Reference
Sequence PMID Reference
CBM
Glycosylation
Other Domains
Domain Order
CAZy family AA2
Sequences
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Length 363aa
Molecular Weight in kDa (experimental) 38 (major band), 31 (minor band) (SDS-PAGE)
Molecular Weight in kDa (predicted) 37.6
Protein Sequence P28314
MKLSLLSTFA AVIIGALALP QGPGGGGSVT CPGGQSTSNS QCCVWFDVLD DLQTNFYQGS KCESPVRKIL RIVFHDAIGF SPALTAAGQF GGGGADGSII AHSNIELAFP ANGGLTDTVE ALRAVGINHG VSFGDLIQFA TAVGMSNCPG SPRLEFLTGR SNSSQPSPPS LIPGPGNTVT AILDRMGDAG FSPDEVVDLL AAHSLASQEG LNSAIFRSPL DSTPQVFDTQ FYIETLLKGT TQPGPSLGFA EELSPFPGEF RMRSDALLAR DSRTACRWQS MTSSNEVMGQ RYRAAMAKMS VLGFDRNALT DCSDVIPSAV SNNAAPVIPG GLTVDDIEVS CPSEPFPEIA TASGPLPSLA PAP
DNA Sequence X69457
CCCACCTGTT CTACTACTAG TCCTCTTCCA TTTGATATTT GAACGCTGTT TCCGAGGTCA AGAACGACAA CTATGAAGCT CTCGCTTTTG TCCACCTTCG CTGCTGTCAT CATCGGTGCC CTCGCTCTAC CCCAGGGTCC TGGAGGAGGC GGGTCAGTCA CTTGCCCCGG TGGACAGTCC ACTTCGAACA GCCAGTGCTG CGTCTGGTTC GACGTTCTAG ACGATCTTCA GACCAACTTC TACCAAGGGT CCAAGTGTGA GAGCCCTGTT CGCAAGATTC TTAGAATTGT TTTCCATGAC GCGATCGGAT TTTCGCCGGC GTTGACTGCT GCTGGTCAAT TCGGTGGTGG AGGAGCTGAT GGCTCCATCA TTGCGCATTC GAACATCGAA TTGGCCTTCC CGGCTAATGG CGGCCTCACC GACACCGTCG AAGCCCTCCG CGCGGTCGGT ATCAACCACG GTGTCTCTTT CGGCGATCTC ATCCAATTCG CCACTGCCGT CGGCATGTCC AACTGCCCTG GCTCTCCCCG ACTTGAGTTC TTGACGGGCA GGAGCAACAG TTCCCAACCC TCCCCTCCTT CGTTGATCCC CGGTCCCGGA AACACTGTCA CTGCTATCTT GGATCGTATG GGCGATGCAG GCTTCAGCCC TGATGAAGTA GTTGACTTGC TTGCTGCGCA TAGTTTGGCT TCTCAGGAGG GTTTGAACTC GGCCATCTTC AGGTCTCCTT TGGACTCGAC CCCTCAAGTT TTCGATACCC AGTTCTACAT TGAGACCTTG CTCAAGGGTA CCACTCAGCC TGGCCCTTCT CTCGGCTTTG CAGAGGAGCT CTCCCCCTTC CCTGGCGAAT TCCGCATGAG GTCCGATGCT CTCTTGGCTC GCGACTCCCG AACCGCCTGC CGATGGCAAT CCATGACCAG CAGCAATGAA GTTATGGGCC AGCGATACCG CGCCGCCATG GCCAAGATGT CTGTTCTCGG CTTCGACAGG AACGCCCTCA CCGATTGCTC TGACGTTATT CCTTCTGCTG TGTCCAACAA CGCTGCTCCT GTTATCCCTG GTGGCCTTAC TGTCGATGAT ATCGAGGTTT CGTGCCCGAG CGAGCCTTTC CCTGAAATTG CTACCGCCTC AGGCCCTCTC CCCTCCCTCG CTCCTGCTCC TTGATCTGGT GAAGATGGTA CATCCTGCTT CTCTCATCAT CCCTCTTAGC TATTTATCCA ATCTATCTAC CTATCTATGC AGTTTCTGTC CACCCTCAGT TGTGAATATG ACTTGGTTAT CTGGGTGTCC G
Cross-references
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GenBank X69457
UniProt P28314
Protein CAA49216
RefSeq Protein
Broad
PDB 1H3J, 1LYK, 1LYC, 1LY9, 1LY8
Entry history
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Entry Name PRX2A_COPCI
Previous Entry Names PRXA_COPCI
Last Modification Date 2013-04-30