Arthromyces ramosus

APX, ascorbate peroxidase PJiP, Arthromyces ramosus peroxidase BPl, barley grain peroxidase CCP, C3dochrome c peroxidase CIP, Coprinus cinereus peroxidase EXAFS, extended X-ray absorption fine structure HRP, horseradish peroxidase HRP Z (where Z = A1-A3, B1-B3, Cl, C2, D, E1-E6, or N), a specific isoenzyme of horseradish peroxidase HS, high-spin lAA, indole-3-acetic acid LIP, hgnin peroxidase LS, low-spin PNP, the major cationic isoenzyme of peanut peroxidase WT, wild-type 5-c, five-coordinate 6-c, six-coordinate. 

Arthritis, gold antiarthritic drugs, 36 17-23 Arthromyces ramosus peroxidase, 43 79 active-site structure, 43 85, 87 crystal structure, 43 84-87 residue location, 43 101-102 van der Waals surfaces, 43 112-113 Aryl... 

Battistuzzi G, Bellei M, De Rienzo F et al (2006) Redox properties of the Fe3+/Fe2+ couple in Arthromyces ramosus class II peroxidase and its cyanide adduct. J Biol Inorg Chem 11 586-592... 

Farhangrazi ZS, Copeland BR, Nakayama T et al (1994) Oxidation-reduction properties of compounds I and II of Arthromyces ramosus peroxidase. Biochemistry 33 5647-5652... 

Huang L, Ortiz de Montellano PR (2007) Arthromyces ramosus peroxidase produces two chlorinating species. Biochem Biophys Res Commun 355 581-586... 

ARP Arthromyces ramosus S. cerevisiae 0.5 mg/L Gouka et al. (personal communication)... 

CPO Chloroperoxidase CPO nonheme chloroperoxidase LiP Lignin peroxidase LiPH2 Lignin peroxidase H2 isozyme MnP Manganese peroxidase CiP Coprinus cinereus peroxidase ARP Arthromyces ramosus peroxidase... 

Besides addition of heme, the influence of culture temperature on heterologous production of peroxidases has also been reported. For example, lowering the culture temperature from 28 to 19°C enhanced the level of active versatile peroxidase of P. eryngii 5.8-fold and reduced the effective proteolytic activity of the A. nidulans host strain by 2-fold. In this way, a maximum peroxidase activity of 466 U/L was reached [42]. Efficient heterologous production of peroxidases is not always dependent on the availability of heme. The heterologous production of Arthromyces ramosus peroxidase (ARP) has been analyzed in A. awamori under the control of the inducible endoxylanase promoter. Secretion of active ARP was achieved at up to 800 mg/L in shake flask cultures without addition of hemin [43]. This represents a 1,600-fold increase in production compared to ARP production in S. cerevisiae and 38-fold increase compared to ARP production in P. pastoris (see Sect. 12.2). These observations support that several filamentous fungi are more effective secretors of proteins than yeast strains like S. cerevisiae and P. pastoris. Also for... 

Lokman BC, Joosten V, Hovenkamp J et al (2003) Efficient production of Arthromyces ramosus peroxidase by Aspergillus awamori. J Biotechnol 103 183-190... 

Abbreviations APX, ascorbate peroxidase pAPX, pea cytosolic APX CcP, cytochrome c peroxidase HRP, horseradish peroxidase Lip, lignin peroxidase MnP, manganese peroxidase PNP, peanut peroxidase ARP, Arthromyces ramosus peroxidase 5-c/HS, 5-coordinate, high-spin heme 6-c/HS, 6-coordinate, high-spin heme 6-c/LS, 6-coordinate, low-spin heme SHE, standard hydrogen electrode. 

TCNQ 7,7,8,8-tetracyanoquinodimethane, TPP tyramine pyrophosphate, ARP peroxidase from Arthromyces ramosus, FAD flavin adenine dinucleotide. 

BIDS diaminodiethyl disulfide PEI-polyethylene imine AAOD Amino acid oxidase ARP Arthromyces ramosus LDL Lower limit of detection LBL Layer by layer SPAN Sulfonated polyaniline. 

Fig. 5. Schematic diagram of Arthromyces ramosus peroxidase C backbone generated from the X-ray coordinates (30). The heme, the distal His56, the proximal Hisl84, the four disulfide bridges, and the van der Waals radii of the two Ca ions are shown in bold.

Fig. 6, The active-site structure of Arthromyces ramosus peroxidase. The dashed lines represent H-bonds between N1 of the distal His56 and the side-chain carbonyl of Asn93, and N1 of the proximal Hisl84 and the side-chain carboxylate of Asp246. This diagram was generated using the X-ray coordinates for the 1.9-A structure of ARP (30).

Hydrogen Peroxide has been shown to be efficiently electroreduced at an electrode modified with a hydrophilic, penneable film of horseradish peroxidase covalently bound to a 3-dimensional epoxy network having polyvinyl pyridine (PVP)-complexed [Os(bpy)2Cl] - redox centers. Four peroxide sensing cathodes based on peroxidases from Arthromyces ramosus, horseradish and bovine milk are compared. Their sensitivity at O.OV (SCE) ranges from 0.1 - 1.0 A cm - M"1, and their limiting currents relate to the enzyme s ability to complex with the redox epoxy network. 

Figure 2. Redox cycles occurring in the 3-dimensional redox epoxy hydrogel. POD represents any of the following enzymes native horseradish peroxidase, NaI04 treated horseradish peroxidase, lactoperoxidase, or Arthromyces ramosus peroxidase.

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