about
Heterologous expression of Pleurotus eryngii peroxidase confirms its ability to oxidize Mn(2+) and different aromatic substratesProtein design: toward functional metalloenzymesBinding Modes of Aromatic Ligands to Mammalian Heme Peroxidases with Associated Functional Implications: CRYSTAL STRUCTURES OF LACTOPEROXIDASE COMPLEXES WITH ACETYLSALICYLIC ACID, SALICYLHYDROXAMIC ACID, AND BENZYLHYDROXAMIC ACIDLigninolytic peroxidase genes in the oyster mushroom genome: heterologous expression, molecular structure, catalytic and stability properties, and lignin-degrading abilityLigand binding reveals a role for heme in translationally-controlled tumor protein dimerization.Improvement of activity and stability of chloroperoxidase by chemical modification.The tautomeric state of histidines in myoglobinExtensive sampling of basidiomycete genomes demonstrates inadequacy of the white-rot/brown-rot paradigm for wood decay fungi.Homologous expression of recombinant lignin peroxidase in Phanerochaete chrysosporiumEfficient heterologous expression in Aspergillus oryzae of a unique dye-decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1.Molecular dynamics simulations of lignin peroxidase in solution.Structural implications of the C-terminal tail in the catalytic and stability properties of manganese peroxidases from ligninolytic fungi.A survey of left-handed polyproline II helicesHomologous expression of recombinant manganese peroxidase in Phanerochaete chrysosporium.Inactivation of myeloperoxidase by benzoic acid hydrazide.Direct interaction of lignin and lignin peroxidase from Phanerochaete chrysosporium.Microbial degradation of lignin: how a bulky recalcitrant polymer is efficiently recycled in nature and how we can take advantage of thisLactoperoxidase: structural insights into the function,ligand binding and inhibition.Quantum mechanical modeling: a tool for the understanding of enzyme reactions.Cloning and characterization of a cDNA encoding a novel extracellular peroxidase from Trametes versicolor.Differential regulation of mnp2, a new manganese peroxidase-encoding gene from the ligninolytic fungus Trametes versicolor PRL 572.Stabilization of lignin peroxidases in white rot fungi by tryptophan.Decolorization of Azo, Triphenyl Methane, Heterocyclic, and Polymeric Dyes by Lignin Peroxidase Isoenzymes from Phanerochaete chrysosporium.The kinetics of the oxidation of cytochrome c by Paracoccus cytochrome c peroxidase.Redox equilibria of manganese peroxidase from Phanerochaetes chrysosporium: functional role of residues on the proximal side of the haem pocket.Direct oxidation of polymeric substrates by multifunctional manganese peroxidase isoenzyme from Pleurotus ostreatus without redox mediatorsOxidation of indole-3-acetic acid by dioxygen catalysed by plant peroxidases: specificity for the enzyme structure.The 2.2 Å resolution structure of the catalase-peroxidase KatG from Synechococcus elongatus PCC7942.The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis.Expression of lignin peroxidase H8 in Escherichia coli: folding and activation of the recombinant enzyme with Ca2+ and haem.Engineering a fungal peroxidase that degrades lignin at very acidic pH.Formation and properties of dimeric recombinant horseradish peroxidase in a system of reversed micellesLuffa aegyptiaca (Gourd) Fruit Juice as a Source of Peroxidase.Cytochrome c3 from Desulfovibrio gigas: crystal structure at 1.8 A resolution and evidence for a specific calcium-binding site.Anionic tobacco peroxidase is active at extremely low pH: veratryl alcohol oxidation with a pH optimum of 1.8.Reversible alkaline inactivation of lignin peroxidase involves the release of both the distal and proximal site calcium ions and bishistidine co-ordination of the haem.Lignin peroxidase ligand access channel dysfunction in the presence of atrazine.Membrane-Bound Class III Peroxidases: Unexpected Enzymes with Exciting Functions
P2860
Q24550544-792E0024-C950-4B33-8454-5471E4E4963AQ26866201-6ECDCA0A-9BEE-467B-968C-C6E125AC70A6Q27655586-A889CB06-BDFE-46F5-B459-E8CBCD48BF3CQ27681166-04216FC8-7933-4106-B25C-EBD0204BDFBFQ30409402-268245B9-ED79-43CF-9B07-42F37322BA95Q33285060-AA9EFEB4-1DD5-4D30-BA21-D4F8634E1081Q33908001-1B9C5AB3-BD45-406E-BE2A-FF1031987025Q33919794-6D1FA501-FBA6-405A-AD29-BF56E05C4B1AQ33984711-18D0C010-8D1A-48F4-A2DB-59110B92815FQ33987070-88421553-6C99-47EC-87C6-588BAAD6CE57Q34181513-CDE4AEC6-2EB0-4DBB-A9B9-069CE1F34444Q34640002-4A95E6F9-C06B-4488-A11B-5EF1D514BFC5Q34646317-4F1F5392-81A4-42C1-802F-FBEF1C795E51Q36061648-0E12EB53-E085-4361-B50A-01A6088DA962Q36654783-E62F1B97-D868-4CB1-A137-39906E665AD0Q37167391-7E8E71DA-C513-4F81-B799-CB73FA78B4E9Q37831986-5F8C4DEB-2A1A-499C-A9C6-479EEF98A228Q38139409-60C1EFE9-6E11-4227-9B24-9023C1D456D0Q38223681-6853A814-2B99-40CE-B041-C3F644D5696EQ39481028-2009A5AC-265E-4E5F-8782-E3C781EA3C2AQ39639563-5C3248D0-1EB1-4B0F-BE3C-870F4645B0F9Q39802454-D0BBA93C-E157-48ED-A543-88886CF1007BQ39894650-D68C32F3-4F26-4B95-972A-5CFB9541167AQ41783811-B5A466FA-61A9-4A11-80F5-A8B509B08C53Q41814263-481299F2-BBA6-4B4F-AD44-13E62AB1C933Q41834141-A3F50D8F-1A92-4B99-AEAF-25C6F7D486FAQ41888087-BFD616D4-4DB5-45AD-9F78-C5CCECEF5892Q41995897-F6CD9D74-053B-4437-ABAB-FD19AC00E6BFQ42115614-193EDD53-F802-48CE-83BC-7DC6042019A6Q42232598-D3758E2D-3A7C-4996-B44C-F4E9B09EC61FQ42286445-48724D89-76AD-42BE-B18B-B4B76A1BE352Q42553546-FC6C1569-2666-4DEF-AA96-F6E3FE15E58EQ42840553-866C8766-1F42-49CE-BF18-E973C9BA0988Q42845388-10C6D575-2D7B-4460-AB8C-14FF0DC0F0F8Q42984666-22053174-12F9-4482-92F7-130E960C6B6CQ42995074-1E59F8E7-F39B-4161-8D64-82A31F1B033DQ53409185-39D67466-A2E0-4231-9DF3-5211C63E8E27Q59138377-5A7D41C3-65A3-489C-A6C0-594A29A2F43C
P2860
description
1993 nî lūn-bûn
@nan
1993 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Crystallographic refinement of lignin peroxidase at 2 A
@ast
Crystallographic refinement of lignin peroxidase at 2 A
@en
Crystallographic refinement of lignin peroxidase at 2 A
@nl
type
label
Crystallographic refinement of lignin peroxidase at 2 A
@ast
Crystallographic refinement of lignin peroxidase at 2 A
@en
Crystallographic refinement of lignin peroxidase at 2 A
@nl
prefLabel
Crystallographic refinement of lignin peroxidase at 2 A
@ast
Crystallographic refinement of lignin peroxidase at 2 A
@en
Crystallographic refinement of lignin peroxidase at 2 A
@nl
P2093
P356
P1476
Crystallographic refinement of lignin peroxidase at 2 A
@en
P2093
H Wariishi
S L Edwards
T L Poulos
P304
P356
10.2210/PDB1LGA/PDB
P407
P577
1993-02-01T00:00:00Z