Prokaryotic Pseudomonas

Muraki T, M Taki, Y Hasegawa, H Iwaki, PCK Lau (2003) Prokaryotic homologues of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7. Appl Environ Microbiol 69 1564-1572. 

E. coli, Bacillus and Pseudomonas present quite a solid base for the production of non-glycosylated proteins. Nevertheless, a number of other prokaryotic expression hosts exist that are not as well established and which show features that are not present in the major expression organisms, and this could be extremely useful for special case proteins. 

Some well-known inhibitors of prokaryotic translation include streptomycin, erythromycin, tetracydine, and chloramphenicol. Inhibitors of eukaryotic translation include cycloheximide and Diphtheria and Pseudomonas toxins. 

Fungi (e.g. Cunninghamella sp., Aspergillus sp., Saccharomyces cerevisiae) are eukaryotic organisms, like mammals, and are the most commonly utilized microorganisms in biotransformation studies [31, 32]. The use of bacteria (prokaryotes) is limited mostly to actinomycetes that seem to contain an enzyme system very similar to that of fungi. Other bacteria (e.g. Pseudomonas, Escherichia coli) are used occasionally, but their usefulness is limited [26, 33]. 

Prokaryote domain (EU) BACTERIA PROTEOBACTERIA Gram-negative bacteria, primitively photosynthetic or chemolithotrophic, with several groups that developed aerobic respiration original source of mitochondria of eukaryotes includes anaerobic PA, chemo-autotrophs (e.g. ammonium oxidisers), oxygen or nitrate respiring H pseudomonads Nitromonas, Pseudomonas... 

ANAFP from A. niger [37], and NAF from PenicilUum nalgiovense [38], From the prokaryotes, examples include the pseudo-mycins and syringomycins produced by Pseudomonas syringae [39, 40] which have both a peptide and a lipid component. 

Figure 8 Examples of protein glycosylation in prokaryotes, (a) Campyiobacter jejuni N-linked glycosylation (b) Pseudomonas aeruginosa pilin O-linked glycosylation (c) C. jejuni and Heiicobacterpyiori O-linked glycosylation (d) Neisseria meningitidis O-linked.

Two mitochondrial isoforms of rat A A -enoyl-CoA isomerase have been described, the first one being a mitochondrial short-chain isomerase with a preferred chain-length specificity of Cg-C. This heat-stable enzyme has a subunit size of 30kDa and a pi value of about 9.5. The second isoform found in rat liver is also mitochondrial, but its catalytic rate is greatest for Cjo-Cn enoyl-CoA substrates and it is not clofibrate-inducible, unlike the rat liver short-ehain specific enzyme. The cDNA sequence of the mitochondrial short-chain isomerase has been published and its amino acid sequence shows similarity to the mitochondrial 2-enoyl-CoA hydratase 1. Currently the hydratase/isomerase family has about 30 known eukaryotic and prokaryotic members and the structure for two members has been published (rat mitochondrial 2-enoyl-CoA hydratase 1 and Pseudomonas sp. 4-chlorobenzoyl-CoA dehalogenase ). They all possess a conserved fingerprint of Val-Ser-X-Ile-Asn-Qy-X-X-X-Ala-Gly-Qy-X-Leu-X-X-X-X-Cys-Asp-Tyr, potentially have similar main chain folding, and catalyze reactions with carboxylic CoA esters as substrates. "... 

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