Literature summary for 1.11.1.16 extracted from

Liu, J.; Zhang, S.; Shi, Q.; Wang, L.; Kong, W.; Yu, H.; Ma, F.
Highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase (2019), Int. Biodeter. Biodegrad., 136, 41-48 .

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Search for more literature for 1.11.1.16

Cloned(Commentary)

Cloned (Comment)	Organism
gene vp1, DNA and amino acid sequence determination and analysis, recombinant overexpression of His-tagged enzyme VP1 in inclusion body in Escherichia coli strain BL21(DE3), most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. The ratio of guaiacyl-type to syringyl-type derivatives (G/S) after rVP1 treatment is 5.4times higher than that of the control	Physisporinus vitreus

Cloned (Comment)

Organism

gene vp1, DNA and amino acid sequence determination and analysis, recombinant overexpression of His-tagged enzyme VP1 in inclusion body in Escherichia coli strain BL21(DE3), most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. The ratio of guaiacyl-type to syringyl-type derivatives (G/S) after rVP1 treatment is 5.4times higher than that of the control

Physisporinus vitreus

Protein Variants

Protein Variants	Comment	Organism
additional information	generation of a recombinant enzyme rVP1 expressed from Escherichia coli in inclusion bodies, renaturation of the recombinant enzyme. Most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. The ratio of guaiacyl-type to syringyl-type derivatives (G/S) after rVP1 treatment is 5.4times higher than that of the control. The polymerization of alkali lignin may be attributed to the transformation of S-type into G-type lignin by demethoxylation	Physisporinus vitreus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Michaelis-Menten steady-state kinetic analysis, recombinant enzyme	Physisporinus vitreus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
extracellular	the enzyme contains a predicted signal peptide	Physisporinus vitreus	-	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mn2+	Mn(II) can promote the oxidation of low redox potential substrates and increase decolorization efficiency up to 70% for the recombinant enzyme VP1 (rVP1), binding site structure analysis	Physisporinus vitreus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Physisporinus vitreus	highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase	?	-	-
additional information	Physisporinus vitreus PF18	highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase	?	-	-

Organism

Organism	UniProt	Comment	Textmining
Physisporinus vitreus	-	-	-
Physisporinus vitreus PF18	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant refolded His-tagged enzyme VP1 from Escherichia coli BL21(DE3) by nickel affinity chromatography	Physisporinus vitreus

Renatured (Commentary)

Renatured (Comment)	Organism
recombinant His-tagged enzyme VP1 from inclusion body from Escherichia coli BL21(DE3)	Physisporinus vitreus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
23.1	-	purified refolded recombinant enzyme VP1, pH and temperature not specified in the publication	Physisporinus vitreus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
2 Mn(II) + 2 H+ + H2O2	-	Physisporinus vitreus	2 Mn(III) + 2 H2O	-	?
2 Mn(II) + 2 H+ + H2O2	-	Physisporinus vitreus PF18	2 Mn(III) + 2 H2O	-	?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H+ + H2O2	-	Physisporinus vitreus	oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + 2 H2O	-	?
2,6-dimethoxyphenol + 2 H+ + H2O2	-	Physisporinus vitreus	oxidized 2,6-dimethoxyphenol + 2 H2O	-	?
2,6-dimethoxyphenol + 2 H+ + H2O2	-	Physisporinus vitreus PF18	oxidized 2,6-dimethoxyphenol + 2 H2O	-	?
indigo carmine + 2 H+ + H2O2	dye decolorization	Physisporinus vitreus	oxidized indigo carmine + 2 H2O	-	?
methyl green + 2 H+ + H2O2	dye decolorization	Physisporinus vitreus	oxidized methyl green + 2 H2O	-	?
additional information	highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase	Physisporinus vitreus	?	-	-
additional information	the enzyme performs decolorization of azo dyes. Most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. Pyrolysis-GC/MS analysis of lignin modified products, detailed overview	Physisporinus vitreus	?	-	-
additional information	highly efficient oxidation of synthetic and natural lignin-related compounds by Physisporinus vitreus versatile peroxidase	Physisporinus vitreus PF18	?	-	-
additional information	the enzyme performs decolorization of azo dyes. Most derivatives of G-type lignin increase slightly by the recombinant enzyme rVP1 treatment compared with the control. Pyrolysis-GC/MS analysis of lignin modified products, detailed overview	Physisporinus vitreus PF18	?	-	-
Reactive Black 5 + 2 H+ + H2O2	dye decolorization	Physisporinus vitreus	oxidized Reactive Black 5 + 2 H2O	-	?
Reactive Black 5 + 2 H+ + H2O2	dye decolorization	Physisporinus vitreus PF18	oxidized Reactive Black 5 + 2 H2O	-	?
Remazol brilliant blue R + 2 H+ + H2O2	dye decolorization	Physisporinus vitreus	oxidized Remazol brilliant blue R + 2 H2O	-	?

Subunits

Subunits	Comment	Organism
?	x * 40000, refolded recombinant enzyme VP1, SDS-PAGE	Physisporinus vitreus

Synonyms

Synonyms	Comment	Organism
VP1	-	Physisporinus vitreus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	30	assay at	Physisporinus vitreus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4.5	-	assay with substrate Mn2+	Physisporinus vitreus
5	-	assay with azo dye substrates	Physisporinus vitreus

Cofactor

Cofactor	Comment	Organism	Structure
heme	binding site structure analysis	Physisporinus vitreus

General Information

General Information	Comment	Organism
additional information	enzyme VP1 contains a Mn-binding site, a heme binding site and a substrate binding site according to the conserved domain database (CDD). VP1 demonstrates both MnP and LiP structural characterization, including Mn-binding site and an exposed tryptophan residue. The conserved Mn-binding site allows VP to obtain electrons from Mn(II) and oxidize Mn(II) to Mn(III). Three conserved amino acid residues, Glu63, Glu67, and Asp202, comprise the Mn-binding site of both VP and MnP. The chelated Mn(III) ions released from the Mn binding site act as diffusible charge transfer mediators attacking low redox potential phenolic substrates like 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 2,6-dimethoxyphenol. According to multiple sequence alignment, the tryptophan residue is conserved in VP1 and other VPs and LiPs, but not in MnPs. Trp191 in VP1 is likely to have a direct oxidation capacity on high redox potential substrates, such as verytryl alcohol and Reactive Black 5 via long-range electron transfer (LRET) to heme. In addition, two conserved residues, His102 and His259, located on the proximal and the distal of heme binding region and conserved in VP and LiP, may also involve in LRET for high redox potential substrates oxidation	Physisporinus vitreus
physiological function	the enzyme performs dye decolorization	Physisporinus vitreus