KEGG   ENZYME: 1.11.1.19Help
Entry
EC 1.11.1.19                Enzyme                                 

Name
dye decolorizing peroxidase;
DyP;
DyP-type peroxidase
Class
Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxidases
BRITE hierarchy
Sysname
Reactive-Blue-5:hydrogen-peroxide oxidoreductase
Reaction(IUBMB)
Reactive Blue 5 + 2 H2O2 = phthalate + 2,2'-disulfonyl azobenzene + 3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate + 2 H2O [RN:R10915]
Reaction(KEGG)
Substrate
Reactive Blue 5 [CPD:C19693];
H2O2 [CPD:C00027]
Product
phthalate [CPD:C01606];
2,2'-disulfonyl azobenzene [CPD:C20938];
3-[(4-amino-6-chloro-1,3,5-triazin-2-yl)amino]benzenesulfonate [CPD:C20939];
H2O [CPD:C00001]
Comment
Heme proteins with proximal histidine secreted by basidiomycetous fungi and eubacteria. They are similar to EC 1.11.1.16 versatile peroxidase (oxidation of Reactive Black 5, phenols, veratryl alcohol), but differ from the latter in their ability to efficiently oxidize a number of recalcitrant anthraquinone dyes, and inability to oxidize Mn(II). The model substrate Reactive Blue 5 is converted with high efficiency via a so far unique mechanism that combines oxidative and hydrolytic steps and leads to the formation of phthalic acid. Bacterial TfuDyP catalyses sulfoxidation.
History
EC 1.11.1.19 created 2011, modified 2015
Orthology
K15733  dye decolorizing peroxidase
Genes
MMC: Mmcs_1602
MKM: Mkms_1626
MJL: Mjls_1572
MYV: G155_29400
MYN: MyAD_21585
MSM: MSMEG_6567
MSG: MSMEI_6390
MSB: LJ00_32465
MSN: LI99_32470
MSH: LI98_32475
MVA: Mvan_2157
MGI: Mflv_4209
MVQ: MYVA_2041
MTHN: 4412656_02086(efeN)
MAB: MAB_2270c
MABB: MASS_2194
MCHE: BB28_11375
MSTE: MSTE_02200
CGL: NCgl1608(Cgl1672)
CGB: cg1881
CGU: WA5_1608
CGT: cgR_1717
CGM: cgp_1881
CGJ: AR0_08855
CEF: CE1786
CDI: DIP1389
CDP: CD241_1331(ycdC)
CDH: CDB402_1300(ycdC)
CDT: CDHC01_1331(ycdC)
CDE: CDHC02_1290(ycdC)
CDR: CDHC03_1310(ycdC)
CDA: CDHC04_1311(ycdC)
CDZ: CD31A_1406(ycdC)
CDB: CDBH8_1383(ycdC)
CDS: CDC7B_1393(ycdC)
CDD: CDCE8392_1306(ycdC)
CDW: CDPW8_1379(ycdC)
CDV: CDVA01_1274(ycdC)
CDIP: ERS451417_01405(ycdC)
CJK: jk1067
CUR: cu0924
COP: Cp31_1200
CPSE: CPTA_01764
CPSU: CPTB_01999
CPSF: CPTC_01755
CRD: CRES_1149
CVA: CVAR_1560
CTER: A606_06195
CSP: WM42_2552
CPHO: CPHO_05385
CGV: CGLAU_07090(efeN)
CAQU: CAQU_07140
CAMG: CAMM_06210
NFR: ERS450000_00996(efeN_1)
RER: RER_11620
REY: O5Y_05305
ROP: ROP_30550
REQ: REQ_10240
RHB: NY08_2786
SCO: SCO3963(SCD78.30c)
SALB: XNR_2920
SGR: SGR_3628
SGB: WQO_17580
SFA: Sfla_3111
SBH: SBI_05287
SVE: SVEN_3736
SALS: SLNWT_3743
STRP: F750_3647
SFI: SFUL_3632
STRM: M444_17435
SPRI: SPRI_3863
SLE: sle_36660(sle_36660) sle_58700(sle_58700)
STRD: NI25_19570
SMAL: SMALA_3813
SALJ: SMD11_3347
SFK: KY5_3984
LXX: Lxx21010
MTS: MTES_2548
AMIN: AUMI_10780
AUW: AURUGA1_01328(efeN)
ARM: ART_3659
KRH: KRH_03680
JDE: Jden_1171
IDO: I598_0264(efeN)
DCO: SAMEA4475696_1082(efeN)
NCA: Noca_2002
NDK: I601_3704(efeN_2)
PSIM: KR76_07090
TFU: Tfu_3078
TCU: Tcur_2987
SRO: Sros_3398
FAL: FRAAL0168
NML: Namu_5006
SESP: BN6_45630
KAL: KALB_2406
SAQ: Sare_2788
MIL: ML5_4729
ACTN: L083_3539(efeB)
AFS: AFR_14045
CAI: Caci_3064
SNA: Snas_2163
 » show all
Taxonomy
Reference
1  [PMID:10049859]
  Authors
Kim SJ, Shoda M
  Title
Purification and characterization of a novel peroxidase from Geotrichum candidum  dec 1 involved in decolorization of dyes.
  Journal
Appl Environ Microbiol 65:1029-35 (1999)
Reference
2  [PMID:15313183]
  Authors
Sugano Y, Ishii Y, Shoda M
  Title
Role of H164 in a unique dye-decolorizing heme peroxidase DyP.
  Journal
Biochem Biophys Res Commun 322:126-32 (2004)
DOI:10.1016/j.bbrc.2004.07.090
Reference
3  [PMID:17654547]
  Authors
Zubieta C, Joseph R, Krishna SS, McMullan D, Kapoor M, Axelrod HL, Miller MD, Abdubek P, Acosta C, Astakhova T, Carlton D, Chiu HJ, Clayton T, Deller MC, Duan L, Elias Y, Elsliger MA, Feuerhelm J, Grzechnik SK, Hale J, Han GW, Jaroszewski L, Jin KK, Klock HE, Knuth MW, Kozbial P, Kumar A, Marciano D, Morse AT, Murphy KD, Nigoghossian E, Okach L, Oommachen S, Reyes R, Rife CL, Schimmel P, Trout CV, van den Bedem H, Weekes D, White A, Xu Q, Hodgson KO, Wooley J, Deacon AM, Godzik A, Lesley SA, Wilson IA
  Title
Identification and structural characterization of heme binding in a novel dye-decolorizing peroxidase, TyrA.
  Journal
Proteins 69:234-43 (2007)
DOI:10.1002/prot.21673
Reference
4  [PMID:19009358]
  Authors
Sugano Y, Matsushima Y, Tsuchiya K, Aoki H, Hirai M, Shoda M
  Title
Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP  from Thanatephorus cucumeris Dec 1.
  Journal
Biodegradation 20:433-40 (2009)
DOI:10.1007/s10532-008-9234-y
Reference
5  [PMID:19099183]
  Authors
Sugano Y
  Title
DyP-type peroxidases comprise a novel heme peroxidase family.
  Journal
Cell Mol Life Sci 66:1387-403 (2009)
DOI:10.1007/s00018-008-8651-8
Reference
6  [PMID:19801472]
  Authors
Ogola HJ, Kamiike T, Hashimoto N, Ashida H, Ishikawa T, Shibata H, Sawa Y
  Title
Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120.
  Journal
Appl Environ Microbiol 75:7509-18 (2009)
DOI:10.1128/AEM.01121-09
Reference
7  [PMID:19967355]
  Authors
van Bloois E, Torres Pazmino DE, Winter RT, Fraaije MW
  Title
A robust and extracellular heme-containing peroxidase from Thermobifida fusca as  prototype of a bacterial peroxidase superfamily.
  Journal
Appl Microbiol Biotechnol 86:1419-30 (2010)
DOI:10.1007/s00253-009-2369-x
  Sequence
[tfu:Tfu_3078]
Reference
8  [PMID:19756587]
  Authors
Liers C, Bobeth C, Pecyna M, Ullrich R, Hofrichter M
  Title
DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes.
  Journal
Appl Microbiol Biotechnol 85:1869-79 (2010)
DOI:10.1007/s00253-009-2173-7
Reference
9  [PMID:20495915]
  Authors
Hofrichter M, Ullrich R, Pecyna MJ, Liers C, Lundell T
  Title
New and classic families of secreted fungal heme peroxidases.
  Journal
Appl Microbiol Biotechnol 87:871-97 (2010)
DOI:10.1007/s00253-010-2633-0
Other DBs
ExplorEnz - The Enzyme Database: 1.11.1.19
IUBMB Enzyme Nomenclature: 1.11.1.19
ExPASy - ENZYME nomenclature database: 1.11.1.19
BRENDA, the Enzyme Database: 1.11.1.19

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