Penicillium vitale

Step 3 is very fast, especially at pH 5, when the enzymatic activity of GO is the highest. The second-order rate constant k i equals 1.6 x 106 M-1 s-1 (23,24) but decreases more than 100-fold at pH>8 (24). Similar pH effect has been reported for GO from Penicillium vitale (25). The oxidation of FADH2 occurs in two le steps. At pH 5.3 the corresponding directly obtained redox potentials for the Aspergillus niger enzyme equal 0.048 and -0.050 V vs. NHE (26). The rate constant k3 is a very important characteristic of GO because a good mediator must oxidize the reduced enzyme not slower than dioxygen. 

Vainshtein BK, Melikadamyan WR, Barynin VV et al (1986) 3-Dimensional structure of catalase from Penicillium vitale at 2.0 A resolution. J Mol Biol 188 49-61... 

Kulys, J.T. and Cenas, N.K. (1983) Oxidation of glucose oxidase from Penicillium vitale by one- and two-electron acceptors. Biochimica et Biophysica Acta, 744, 57-63. 

Kulys J J and Cenas N K 1983 Oxidation of glucose oxidase Penicillium vitale... 

Kulys, J. J., Cenas, N. K., Oxidation of Glucose Oxidase from Penicillium Vitale by One- and TVvo-Electron Acceptors , Biochim. Biophys. Acta 744 (1983) 57-63. 

Murshudov GN, Grebenko AI, Barynin V, Dauter Z, Wilson KS, Vainshtein BK, Melik-Adamyan W, Bravo J, Ferran JM, Ferrer JC, Switala J, Loewen PC, Fita I (1996) Structure of the Heme d of Penicillium vitale and Escherichia coli Catalases. J Biol Chem 271 8863... 

The mold from which Fleming discovered penicillin was Penicillium notatum, a strain that gives a relatively low yield of penicillin. Commercial production of the antibiotic uses P. chrysogenum, a strain cultured from a mold found growing on a grapefruit in a market in Peoria, Illinois. The penicillins owe their antibacterial activity to a common mechanism that inhibits the biosynthesis of a vital part of bacterial cell walls. 

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