EC number:1.11.2.4

Enzyme

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     1. Oxidoreductases
        1.11 Acting on a peroxide as acceptor
            1.11.2 Peroxygenases
ID:1.11.2.4
Description:Fatty-acid peroxygenase.
Alternative Name: P450SP-alpha.
P450 peroxygenase.
Fatty acid hydroxylase.
CYP152A1.
Prosite: PDOC00081;
PDB:
PDBScop
4RUI 8068640; 8068641; 8068640; 8068641; 8068640; 8068641; 8068640; 8068641; 8068640; 8068641; 8068640; 8068641;
4EJJ 8068640; 8068641; 8068640; 8068641; 8068640; 8068641; 8068640; 8068641;
3T3R 8068640; 8068641; 8068640; 8068641; 8068640; 8068641; 8068640; 8068641;
3T3Q 8068640; 8068641; 8068640; 8068641; 8068640; 8068641; 8068640; 8068641;
3EBS 8068640; 8068641; 8068640; 8068641; 8068640; 8068641; 8068640; 8068641;
 » show all
Cath: 1.10.630.10;

3D structure

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PDB

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4RUI; 4EJJ; 3T3R; 3T3Q; 3EBS; 2FDY; 2FDW; 2FDV; 2FDU; 1Z11; 1Z10; 1BVY; 2IJ7; 2IJ5; 5OP9; 5IBJ; 5IBI; 5IBH; 5IBG; 5IBF; 5IBE; 5IBD; 4IQ9; 4IQ7; 4IPW; 4IPS; 4ICT; 4G48; 4G47; 4G46; 4G45; 4G44; 4G2G; 4G1X; 3G5H; 3G5F; 3CY1; 3CY0; 3CXZ; 3CXY; 3CXV; 1N4G; 1N40; 1LGF; 1LG9; 1LFK; 5DE9; 3TZO; 1SE6; 2D0E; 2D09; 1T93; 1S1F; 1J51; 4JX1; 4JWS; 4L4C; 4G3R; 4EK1; 3WRM; 3WRL; 3WRK; 3WRJ; 3WRI; 3WRH; 3FWG; 2H7S; 2GR6; 2GQX; 2FRZ; 2FEU; 2A1O; 2A1N; 2A1M; 1UYU; 1T88; 1T87; 1T86; 1O76; 1MPW; 1K2O; 1DZ9; 1DZ8; 1DZ6; 1DZ4; 1C8J; 5GXG; 3W9C; 2M56; 8CPP; 7CPP; 6CPP; 6CP4; 5WK9; 5WK7; 5IK1; 5CPP; 5CP4; 4L4G; 4L4F; 4L4E; 4L4D; 4L4B; 4L4A; 4L49; 4KKY; 4CPP; 4CP4; 3P6X; 3P6W; 3P6V; 3P6U; 3P6T; 3P6S; 3P6R; 3P6Q; 3P6P; 3P6O; 3P6N; 3P6M; 3OL5; 3OIA; 3L63; 3L62; 3L61; 3CPP; 3CP4; 2ZWU; 2ZWT; 2ZUJ; 2ZUI; 2ZUH; 2ZAX; 2ZAW; 2Z97; 2QBO; 2QBN; 2QBM; 2QBL; 2LQD; 2L8M; 2H7R; 2H7Q; 2FER; 2FE6; 2CPP; 2CP4; 1YRD; 1YRC; 1T85; 1RF9; 1RE9; 1QMQ; 1PHG; 1PHF; 1PHE; 1PHD; 1PHC; 1PHB; 1PHA; 1P7R; 1P2Y; 1NOO; 1LWL; 1IWK; 1IWJ; 1IWI; 1GEM; 1GEK; 1GEB; 1CP4; 1AKD; 1UED; 3B4X; 1UE8; 4K9W; 2V0M; 5TE8; 3NXU; 2J0D; 6BDM; 6BDK; 6BDI; 6BDH; 6BD8; 6BD7; 6BD6; 6BD5; 6BCZ; 5VCG; 5VCE; 5VCD; 5VCC; 5VC0; 5G5J; 5A1R; 5A1P; 4NY4; 4K9X; 4K9V; 4K9U; 4K9T; 4I4H; 4I4G; 4I3Q; 4D7D; 4D78; 4D75; 4D6Z; 3UA1; 3TJS; 1W0G; 1W0F; 1W0E; 1TQN; 3DL9; 3CZH; 3C6G; 3EJE; 3EJD; 3EJB; 5JQV; 5JQU; 2UWH; 5ZLH; 5ZIS; 5XA3; 5E9Z; 4H24; 4DUF; 1SMJ; 1FAG; 6H1S; 6H1O; 5XHJ; 5OG9; 5JTD; 5JQ2; 5E7Y; 5E78; 5DYZ; 5DYP; 5B2Y; 5B2X; 5B2W; 5B2V; 5B2U; 4RSN; 4O4P; 4KPB; 4KF2; 4KF0; 4KEY; 4KEW; 4HGJ; 4HGI; 4HGH; 4HGG; 4HGF; 4DUE; 4DUD; 4DUC; 4DUB; 4DUA; 4DU2; 4DTZ; 4DTY; 4DTW; 3WSP; 3PSX; 3NPL; 3M4V; 3KX5; 3KX3; 3HF2; 3EKF; 3EKD; 3EKB; 3DGI; 3CBD; 3BEN; 2X80; 2X7Y; 2NNB; 2J4S; 2J1M; 2IJ4; 2IJ3; 2IJ2; 2HPD; 2BMH; 1ZOA; 1ZO9; 1ZO4; 1YQP; 1YQO; 1SMI; 1P0W; 1JPZ; 1FAH; 1BU7; 4ZFB; 4ZFA; 4ZF8; 4ZF6; 4KPA; 3R1A; 2Q6N; 3TK3; 3R1B; 3ME6; 3G93; 3G5N; 5IUZ; 5EM4; 3MVR; 5IUT; 4JLT; 4H1N; 3UAS; 3TMZ; 3KW4; 2BDM; 1SUO; 1PO5; 4NZ2; 1OG5; 1OG2; 5XXI; 5X24; 5X23; 5W0C; 5K7K; 5A5J; 5A5I; 1R9O; 4WPD; 1IO9; 1IO8; 1IO7; 1F4U; 1F4T; 4WQJ; 4TUV; 4TT5; 2BZ9; 2W0B; 2W0A; 2W09; 2VKU; 2CIB; 2CI0; 1X8V; 1U13; 1H5Z; 1EA1; 1E9X; 1CPT; 5Y5M; 5Y5L; 5Y5K; 5Y5J; 5Y5I; 5Y5H; 5Y5G; 5Y5F; 2ROM; 1XQD; 1ULW; 1ROM; 1JFC; 1JFB; 1GEJ; 1GEI; 1GED; 1F26; 1F25; 1F24; 1EHG; 1EHF; 1EHE; 1CMN; 1CMJ; 1CL6; 1NR6; 1N6B; 1DT6; 1Z8Q; 1Z8P; 1Z8O; 1OXA; 1JIP; 1JIO; 1JIN; 1EUP; 1EGY; 2NNH; 1PQ2; 2VN0; 2NNJ; 2NNI; 6NBL; 4JWU; 6M7X; 6IQ5; 6FMO; 6DWN; 6DWM; 6CSD; 6CSB; 6CIZ; 6CIR; 6CHI; 6B11; 5YM3; 5YLW; 5XNT; 5X7E; 5WBG; 5VEU; 5V5Z; 5UYS; 5UHU; 5UFG; 5UEC; 5UDA; 5UAP; 5TZ1; 5TFU; 5TFT; 5T6Q; 5OMU; 5OMS; 5OMR; 5NCB; 5LIE; 5LI8; 5LI7; 5LI6; 5L1W; 5L1V; 5L1U; 5L1T; 5L1S; 5L1R; 5L1Q; 5L1P; 5L1O; 5JLC; 5JL9; 5JL7; 5JL6; 5JKW; 5JKV; 5IRV; 5IRQ; 5IKI; 5HDI; 5GNM; 5GNL; 5FSA; 5FOI; 5EQB; 5EDT; 5AJR; 4ZV8; 4ZGX; 4YZR; 4YT3; 4Y8W; 4XRZ; 4XRY; 4WNW; 4WNV; 4WNU; 4WNT; 4UVR; 4UQH; 4UMZ; 4UHL; 4UHI; 4UBS; 4UAX; 4TRI; 4RRT; 4RQL; 4RM4; 4NKZ; 4NKY; 4NKX; 4NKW; 4NKV; 4LXJ; 4KQ8; 4J14; 4I91; 4I8V; 4H6O; 4GQS; 4GL7; 4GL5; 4FIA; 4FDH; 4ENH; 4EJI; 4EJH; 4EJG; 4DVQ; 4DNJ; 4COH; 4CKA; 4CK9; 4CK8; 4C28; 4C27; 4C0C; 4BY0; 4BMM; 4BF4; 4B7S; 4B7D; 4AW3; 3ZSN; 3ZPI; 3ZKP; 3ZK5; 3ZG3; 3ZG2; 3ZBY; 3VRM; 3V8D; 3UA5; 3TDA; 3TBG; 3T3Z; 3T3S; 3SWZ; 3SN5; 3S7S; 3S79; 3RUK; 3QZ1; 3QU8; 3QOA; 3QM4; 3PM0; 3NC7; 3NC6; 3NC5; 3NC3; 3NA1; 3NA0; 3N9Z; 3N9Y; 3MZS; 3MDV; 3MDT; 3MDR; 3MDM; 3LD6; 3LC4; 3KSW; 3KOH; 3KHM; 3K9Y; 3K9V; 3K1O; 3JUV; 3JUS; 3IBD; 3GPH; 3EQM; 3E6I; 3E4E; 3DAX; 3CV9; 3CV8; 3A51; 3A50; 3A4Z; 3A4H; 3A4G; 2ZBZ; 2ZBY; 2ZBX; 2YOO; 2YGX; 2YCA; 2Y98; 2Y5Z; 2Y5N; 2Y46; 2XKR; 2XFH; 2WX2; 2WUZ; 2WIO; 2WI9; 2WHW; 2WHF; 2WH8; 2WGY; 2VZM; 2VZ7; 2VE4; 2VE3; 2UVN; 2UUQ; 2Q9G; 2Q9F; 2PG7; 2PG6; 2PG5; 2P85; 2JJP; 2JJO; 2JJN; 2HI4; 2FR7; 2F9Q; 2CD8; 2CA0; 2C7X; 2C6H; 2BVJ; 1GJM;

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.11.2.4
BRENDA Enzyme Link: BRENDA 1.11.2.4
KEGG Enzyme Link: KEGG1.11.2.4
BioCyc Enzyme Link: BioCyc 1.11.2.4
ExPASy Enzyme Link: ExPASy1.11.2.4
EC2PDB Enzyme Link: EC2PDB 1.11.2.4
ExplorEnz Enzyme Link: ExplorEnz 1.11.2.4
PRIAM enzyme-specific profiles Link: PRIAM 1.11.2.4
IntEnz Enzyme Link: IntEnz 1.11.2.4
MEDLINE Enzyme Link: MEDLINE 1.11.2.4

EC number:1.11.2.4

MSA:

1.11.2.4;
Phylogenetic Tree:

1.11.2.4;
Uniprot:
M-CSA:
RHEA:46024 H2O2 + tetradecanoate = (3R)-hydroxytetradecanoate + H2O
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[OH;+0:4]-[OH;+0:5]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[OH2;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid beta-hydroxylating cytochrome P450.Matsunaga I, Ueda A, Fujiwara N, Sumimoto T, Ichihara K1999 Aug10529095
RHEA:46028 H2O2 + tetradecanoate = (2R)-hydroxytetradecanoate + H2O
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[OH;+0:4]-[OH;+0:5]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[OH2;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid beta-hydroxylating cytochrome P450.Matsunaga I, Ueda A, Fujiwara N, Sumimoto T, Ichihara K1999 Aug10529095
RHEA:46032 H2O2 + tetradecanoate = (2S)-hydroxytetradecanoate + H2O
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[OH;+0:4]-[OH;+0:5]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[OH2;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid beta-hydroxylating cytochrome P450.Matsunaga I, Ueda A, Fujiwara N, Sumimoto T, Ichihara K1999 Aug10529095
RHEA:48360 1,2-saturated fatty acid + H2O2 = 2-hydroxy fatty acid + H2O
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[OH;+0:4]-[OH;+0:5]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[OH2;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Further characterization of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis.Matsunaga I, Yamada M, Kusunose E, Miki T, Ichihara K1998 Jul9644252
Direct involvement of hydrogen peroxide in bacterial alpha-hydroxylation of fatty acid.Matsunaga I, Yamada M, Kusunose E, Nishiuchi Y, Yano I, Ichihara K1996 May 208647293
Aromatic C-H bond hydroxylation by P450 peroxygenases: a facile colorimetric assay for monooxygenation activities of enzymes based on Russig's blue formation.Shoji O, Wiese C, Fujishiro T, Shirataki C, Wünsch B, Watanabe Y2010 Sep20490877
Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes.Matsunaga I, Shiro Y2004 Apr15062772
Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies.Lee DS, Yamada A, Sugimoto H, Matsunaga I, Ogura H, Ichihara K, Adachi S, Park SY, Shiro Y2003 Mar 1412519760
Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy.Matsunaga I, Yamada A, Lee DS, Obayashi E, Fujiwara N, Kobayashi K, Ogura H, Shiro Y2002 Feb 1211827534
Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis (peroxygenase P450(SPalpha).Imai Y, Matsunaga I, Kusunose E, Ichihara K2000 Aug10920253
Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid beta-hydroxylating cytochrome P450.Matsunaga I, Ueda A, Fujiwara N, Sumimoto T, Ichihara K1999 Aug10529095
RHEA:48384 2,3-saturated fatty acid + H2O2 = 3-hydroxy fatty acid + H2O
RULE(radius=1) [*:1]-[CH2;+0:2]-[*:3].[OH;+0:4]-[OH;+0:5]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[OH2;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Further characterization of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis.Matsunaga I, Yamada M, Kusunose E, Miki T, Ichihara K1998 Jul9644252
Direct involvement of hydrogen peroxide in bacterial alpha-hydroxylation of fatty acid.Matsunaga I, Yamada M, Kusunose E, Nishiuchi Y, Yano I, Ichihara K1996 May 208647293
Aromatic C-H bond hydroxylation by P450 peroxygenases: a facile colorimetric assay for monooxygenation activities of enzymes based on Russig's blue formation.Shoji O, Wiese C, Fujishiro T, Shirataki C, Wünsch B, Watanabe Y2010 Sep20490877
Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes.Matsunaga I, Shiro Y2004 Apr15062772
Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. Crystallographic, spectroscopic, and mutational studies.Lee DS, Yamada A, Sugimoto H, Matsunaga I, Ogura H, Ichihara K, Adachi S, Park SY, Shiro Y2003 Mar 1412519760
Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy.Matsunaga I, Yamada A, Lee DS, Obayashi E, Fujiwara N, Kobayashi K, Ogura H, Shiro Y2002 Feb 1211827534
Unique heme environment at the putative distal region of hydrogen peroxide-dependent fatty acid alpha-hydroxylase from Sphingomonas paucimobilis (peroxygenase P450(SPalpha).Imai Y, Matsunaga I, Kusunose E, Ichihara K2000 Aug10920253
Characterization of the ybdT gene product of Bacillus subtilis: novel fatty acid beta-hydroxylating cytochrome P450.Matsunaga I, Ueda A, Fujiwara N, Sumimoto T, Ichihara K1999 Aug10529095