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Literature summary for 1.11.1.16 extracted from

  • Sanchez-Alejandro, F.; Baratto, M.C.; Basosi, R.; Graeve, O.; Vazquez-Duhalt, R.
    Addition of new catalytic sites on the surface of versatile peroxidase for enhancement of LRET catalysis (2019), Enzyme Microb. Technol., 131, 109429 .
    View publication on PubMed
Search for more literature for 1.11.1.16

Protein Variants

Protein Variants Comment Organism
additional information introduction of radical-forming aromatic amino acids by chemical modification of the protein surface is performed using carbodiimide and succiniimide as carboxyl group activators, and the catalytic implications of these additional surface active-sites on the oxidation of 2,6-dimethylphenol, Mn2+, and remazol brilliant blue R (RBBR) are determined. These three different substrates are oxidized in different active sites of the enzyme molecule, of which the high redox RBBR is the only one that is transformed by an external radical formed in the protein surface. Both catalytic constants kcat and KM are significantly affected by the chemical modifications. Tryptophan- and tyrosine-modified versatile peroxidase shows higher catalytic transformation than the unmodified enzyme for RBBR, while the Mn2+ oxidation is significantly reduced by all chemical modifications. Formation of additional protein-based radicals after the chemical modification with radical-forming amino acids is determined by electron paramagnetic resonance studies. The chemical modification could modify any free amino or free carboxylic groups. The access channel to the heme edge is formed by two lysines (K212 and K275) and a glutamic acid (E169) that are prone to be modified. Method overview Bjerkandera adusta

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Bjerkandera adusta

Organism

Organism UniProt Comment Textmining
Bjerkandera adusta Q3SC77
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 Mn(II) + 2 H+ + H2O2 oxidation of Mn2+ to Mn3+ (manganese peroxidase activity) is measured as the H2O2-dependent formation of the complex malonate-Mn3+ Bjerkandera adusta 2 Mn(III) + 2 H2O
-
 ?
2,6-dimethoxyphenol + 2 H+ + H2O2 substrate 2,6-dimethoxyphenol (DMP) is transformed at the distal site of heme prosthetic group (lignin peroxidase activity) Bjerkandera adusta oxidized 2,6-dimethoxyphenol + 2 H2O
-
 ?
additional information the oxidation of 2,6-dimethylphenol, Mn2+ and remazol brilliant blue R (RBBR) of the three different substrates occurs at different active sites of the enzyme molecule. Versatile peroxidase (VP) from Bjerkandera adusta is an enzyme able to oxidize bulky and high-redox substrates trough a long-range electron t (LRET) pathway. The catalytic rate of the LRET mediated transformation shows a good correlation with the ionization energy of the additional amino acid on the protein surface Bjerkandera adusta ?
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-
remazol brilliant blue R + H2O2 transformation of the bulky substrate remazol brilliant blue R (RBBR), is monitored at its maximum visible absorbance wavelength of 590 nm Bjerkandera adusta ? + 2 H2O
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
 assay at Bjerkandera adusta

Cofactor

Cofactor Comment Organism Structure
heme prosthetic group Bjerkandera adusta

General Information

General Information Comment Organism
additional information versatile peroxidase (VP) from Bjerkandera adusta is able to oxidize bulky and high-redox substrates through a long-range electron transfer (LRET) pathway Bjerkandera adusta