Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Nomenclature changes of pediococci postdate the publication of Bergey's Manual. Pediococci possess both a "group" and a "type" antigen. They are gram positive, asporogenous, nonmotile, generally catalase negative, but may possess catalase-like activity. The pediococci may have either a cytochrome or a flavoprotein enzyme system. Anaerobically they are homofermentative using the PEP:PTS and the EMP pathway. Catalase positive strains utilize glucose aerobically and anaerobically while lactose and glycerol are only used aerobically. Some pentoses are fermented to lactate and acetate. Absolute requirement for folinic acid and nearly all amino acids is observed. Pediococci grow luxuriously in All Purpose Tween (APT) broth and are isolated on Rogosa SL agar. Detection can be done by electrical impedance and fluorescent antibody techniques. The Arrhenius concept was utilized in selecting metabolically efficient strains. Antibiotics, antioxidants, some chloride salts and some spices are detrimental to the pediococci. On the other hand, some chloride salts, manganese, and some spices are stimulant. Dialysis-fermentation and immobilization of pediococcal cells were recorded. Some strains decarboxylate histidine to histamine. The resting cell metabolism and the production of bacteriocin have been utilized in antibiosis. An intra and intergeneric genetic transfer system of plasmids from pediococci was by a conjugation-like mechanism. Formation of bacteriocin and fermentation of carbohydrates were linked to plasmids. Lytic bacteriophages to pediococci have not yet been identified. Industrial cultures are mainly frozen concentrates. Linear equations were developed to model the fermentative activity of pediococci and the effects of environmental factors.
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PMID:Pediococci and biotechnology. 330 17

Many peroxisomal proteins are imported into peroxisomes via recognition of the peroxisomal targeting signal (PTS1) present at the C-termini by the PTS1 receptor (Pex5p). Catalase, a peroxisomal protein, has PTS1-like motifs around or at the C-terminus. However, it remains unclear whether catalase is imported into peroxisome via the PTS1 system. In this work, we analyzed the PTS of pumpkin catalase (Cat1). A full or truncated pumpkin Cat1 cDNA fused at the 3' end of the green fluorescent protein (GFP) coding sequence was introduced and stably expressed in tobacco BY-2 (Nicotiana tabacum cv. Bright Yellow 2) cells or Arabidopsis thaliana by Agrobacterium-mediated transformation. The cellular localization of GFP was analyzed by fluorescence microscopy. The results showed that the C-terminal 10-amino acid region containing an SKL motif-like tripeptide (SHL) was not required for the import into peroxisomes. Surprisingly, the C-terminal 3-amino acid region was required for the import when the fusion proteins were transiently expressed by using particle gun bombardment, suggesting that the transient expression system is inadequate to analyze the targeting signal. We proposed that the C-terminal amino acid region from 13 to 11 (QKL), which corresponds with the PTS1 consensus sequence, may function as an internal PTS1. Analysis of the binding of Cat1 to PTS1 receptor (Pex5p) by the yeast two-hybrid system revealed that Cat1 can bind with the PTS1 receptor (Pex5p), indicating that Cat1 is imported into peroxisomes by the PTS1 system.
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PMID:Identification of peroxisomal targeting signal of pumpkin catalase and the binding analysis with PTS1 receptor. 1294 50