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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 8005 / IAM11001;
PubMed=2670897 [NCBI, ExPASy, EBI, Israel, Japan]
Loprasert S.,
Negoro S.,
Okada H.;
"Cloning, nucleotide sequence, and expression in Escherichia coli of the Bacillus stearothermophilus peroxidase gene (perA).";
J. Bacteriol. 171:4871-4875(1989).
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[2]
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SEQUENCE REVISION.
Trakulnaleamsai S.,
Aihara S.,
Miyai K.,
Suga Y.,
Yomo T.,
Negoro S.,
Urabe I.;
Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1038/5232; PubMed=9920270 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuura T.,
Miyai K.,
Trakulnaleaamsai S.,
Yomo T.,
Shima Y.,
Miki S.,
Yamamoto K.,
Urabe I.;
"Evolutionary molecular engineering by random elongation mutagenesis.";
Nat. Biotechnol. 17:58-61(1998).
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[4]
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BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1016/j.abb.2007.12.008; PubMed=18178143 [NCBI, ExPASy, EBI, Israel, Japan]
Singh R.,
Wiseman B.,
Deemagarn T.,
Jha V.,
Switala J.,
Loewen P.C.;
"Comparative study of catalase-peroxidases (KatGs).";
Arch. Biochem. Biophys. 471:207-214(2008).
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- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activity.
- CATALYTIC ACTIVITY: 2 H2O2 = O2 + 2 H2O.
- CATALYTIC ACTIVITY: Donor + H2O2 = oxidized donor + 2 H2O.
- COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer.
- BIOPHYSICOCHEMICAL PROPERTIES:
| Kinetic parameters: |
KM=90 mM for H2O2 for the catalase reaction (at pH 5.5-6.0); | | KM=3.7 mM for H2O2 for the catalase reaction (at pH 7.0); | | KM=210 mM for H2O2 for the peroxidase reaction; | | KM=31 mM for ABTS for the peroxidase reaction; | | Vmax=5670 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0); | | Vmax=3410 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0); | | Vmax=8 µmol/min/mg enzyme for ABTS for the peroxidase reaction; | | pH dependence: |
Optimum pH is 4.0 for the peroxidase reaction; | |
- SUBUNIT: Homodimer or homotetramer (By similarity).
- PTM: The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme (By similarity).
- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 735 AA [This is the length of the unprocessed precursor] |
Molecular weight: 82989 Da [This is the MW of the unprocessed precursor] |
CRC64: 7131204A4BFABEF1 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MENQNRQNAA QCPFHGSVTN QSSNRTTNKD WWPNQLNLSI LHQHDRKTNP HDEEFNYAEE
70 80 90 100 110 120
FQKLDYWALK EDLRKLMTES QDWWPADYGH YGPLFIRMAW HSAGTYRIGD GRGGASTGTQ
130 140 150 160 170 180
RFAPLNSWPD NANLDKARRL LWPIKKKYGN KISWADLFIL AGNVAIESMG GKTIGFGGGR
190 200 210 220 230 240
VDVWHPEEDV YWGSEKEWLA SERYSGDREL ENPLAAVQMG LIYVNPEGPD GKPDPKAAAR
250 260 270 280 290 300
DIRETFRRMG MNDEETVALI AGGHTFGKAH GAGPATHVGP EPEAAPIEAQ GLGWISSYGK
310 320 330 340 350 360
GKGSDTITSG IEGAWTPTPT QWDTSYFDML FGYDWWLTKS PAGAWQWMAV DPDEKDLAPD
370 380 390 400 410 420
AEDPSKKVPT MMMTTDLALR FDPEYEKIAR RFHQNPEEFA EAFARAWFKL THRDMGPKTR
430 440 450 460 470 480
YLGPEVPKED FIWQDPIPEV DYELTEAEIE EIKAKILNSG LTVSELVKTA WASASTFRNS
490 500 510 520 530 540
DKRGGANGAR IRLAPQKDWE VNEPERLAKV LSVYEDIQRE LPKKVSIADL IVLGGSAAVE
550 560 570 580 590 600
KAARDAGFDV KVPFFPGRGD ATQEQTDVES FAVLEPFADG FRNYQKQEYS VPPEELLVDK
610 620 630 640 650 660
AQLLGLTAPE MTVLVGGLRV LGANYRDLPH GVFTDRIGVL TNDFFVNLLD MNYEWVPTDS
670 680 690 700 710 720
GIYEIRDRKT GEVRWTATRV DLIFGSNSIL RSYAEFYAQD DNQEKFVRDF INAWVKVMNA
730
DRFDLVKKAR ESVTA
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P14412 in FASTA format |
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