Sequence of LIG2_PHACH
EC Number:1.11.1.14
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = 3,4-dimethoxybenzaldehyde + 2-methoxyphenol + glycolaldehyde + H2O
Other sequences found for EC No. 1.11.1.14
General information:
Sequence
0 MAFKQLFAAI TVALSLTAAN AAVVKEKRAT CANGKTVGDA SCCAWFDVLD DIQANMFHGG
60 QCGAEAHESI RLVFHDSIAI SPAMEAKGKF GGGGADGSIM IFDTIETAFH PNIGLDEVVA
120 MQKPFVQKHG VTPGDFIAFA GAVALSNCPG APQMNFFTGR KPATQPAPDG LVPEPFHTVD
180 QIIARVNDAG EFDELELVWM LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQFRG
240 TLFPGSGGNQ GEVESGMAGE IRIQTDHTLA RDSRTACEWQ SFVGNQSKLV DDFQFIFLAL
300 TQLGQDPNAM TDCSDVIPLS KPIPGNGPFS FFPPGKSHSD IEQACAETPF PSLVTLPGPA
360 TSVARIPPHK A
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
564563
Ritch T.G. Jr.,Nipper V.J.,Akileswaran L.,Smith A.J.,Pribnow D.G.,Gold M.H.
Lignin peroxidase from the basidiomycete Phanerochaete chrysosporium is synthesized as a preproenzyme.
Gene
107
119-126
1991
564564
Ritch T.G. Jr.,Gold M.H.
Characterization of a highly expressed lignin peroxidase-encoding gene from the basidiomycete Phanerochaete chrysosporium.
Gene
118
73-80
1992
564565
Poulos T.L.,Edwards S.L.,Wariishi H.,Gold M.H.
Crystallographic refinement of lignin peroxidase at 2 A.
J. Biol. Chem.
268
4429-4440
1993
564566
Choinowski T.,Blodig W.,Winterhalter K.H.,Piontek K.
The crystal structure of lignin peroxidase at 1.70-A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle.
J. Mol. Biol.
286
809-827
1999
