Photoinduction of phenylalanine deaminase in gherkin seedlings

G. Engelsma

doi:10.1007/bf00387559

Rapid Test for Urease and Phenylalanine Deaminase Production

Applied Microbiology ◽

10.1128/aem.21.3.545-545.1971 ◽

1971 ◽

Vol 21 (3) ◽

pp. 545-545 ◽

Cited By ~ 10

Author(s):

Grace Mary Ederer ◽

Jackie H. Chu ◽

Donna J. Blazevic

Keyword(s):

Rapid Test ◽

Phenylalanine Deaminase

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Paenibacillus favisporus sp. nov., a xylanolytic bacterium isolated from cow faeces

INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY ◽

10.1099/ijs.0.02709-0 ◽

2004 ◽

Vol 54 (1) ◽

pp. 59-64 ◽

Cited By ~ 54

Author(s):

Encarna Velázquez ◽

Trinidad de Miguel ◽

Margarita Poza ◽

Raúl Rivas ◽

Ramón Rosselló-Mora ◽

...

Keyword(s):

Novel Species ◽

Hydrolytic Enzymes ◽

Gas Production ◽

Cow Dung ◽

Rrna Gene ◽

The Novel ◽

Closely Related Species ◽

Main Fatty Acid ◽

Phenylalanine Deaminase ◽

Micro Organisms

During a search for xylan-degrading micro-organisms, a sporulated bacterium was recovered from recent and old cow dung and rectal samples. The isolates were identified as members of a novel species of the genus Paenibacillus, based on 16S rRNA gene sequences. According to the results of phylogenetic analysis, the most closely related species was Paenibacillus azoreducens. Phenotypic and chemotaxonomic analyses and DNA–DNA hybridization experiments also showed that the isolates belonged to a novel species of the genus Paenibacillus. The novel species is a facultatively anaerobic, motile, Gram-variable, sporulated rod. The spores of this rod-shaped micro-organism occur in slightly swollen sporangia and are honeycomb-shaped. The main fatty acid is anteiso-branched C15 : 0. Growth was observed with many carbohydrates, including xylan, as the only carbon source and gas production was not observed from glucose. The novel species produces a wide variety of hydrolytic enzymes, such as xylanases, cellulases, amylases, gelatinase, urease and β-galactosidase. On the contrary, it does not produce caseinase, phenylalanine deaminase or lysine decarboxylase. According to the data obtained in this work, the strains belong to a novel species, for which the name Paenibacillus favisporus sp. nov. is proposed (type strain, GMP01T=LMG 20987T=CECT 5760T).

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Chromohalobacter salarius sp. nov., a moderately halophilic bacterium isolated from a solar saltern in Cabo de Gata, Almería, southern Spain

INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY ◽

10.1099/ijs.0.64953-0 ◽

2007 ◽

Vol 57 (6) ◽

pp. 1238-1242 ◽

Cited By ~ 21

Author(s):

Margarita Aguilera ◽

Antonio Cabrera ◽

Claudia Incerti ◽

Susana Fuentes ◽

Nick J. Russell ◽

...

Keyword(s):

Halophilic Bacterium ◽

Southern Spain ◽

Rrna Gene ◽

Solar Saltern ◽

Moderately Halophilic ◽

Moderately Halophilic Bacterium ◽

Phenylalanine Deaminase ◽

Bacterium Strain ◽

Wildlife Reserve ◽

Type Strains

A moderately halophilic, Gram-negative bacterium (strain CG4.1T), which was isolated from a solar saltern at Cabo de Gata, a wildlife reserve located in the province of Almería, southern Spain, was subjected to a polyphasic taxonomic study. This organism was an aerobic, motile rod that produced colonies with a yellow pigment. Strain CG4.1T grew at salinities of 3–25 % (w/v), at 15–45 °C and at pH 5–9. The organism reduced nitrate, hydrolysed starch and had phenylalanine deaminase activity. The major fatty acids were C18 : 1 ω7c, C16 : 0 and C19 : 0 cyclo ω8c. The DNA G+C content was 63.6 mol%. On the basis of phenotypic and phylogenetic data, strain CG4.1T appears to be a member of the genus Chromohalobacter and clustered closely with Chromohalobacter species, with 95–96 % similarity between their 16S rRNA gene sequences. However, DNA–DNA relatedness between the isolate and the type strains of Chromohalobacter species was low. Therefore, it is proposed that strain CG4.1T represents a novel species, Chromohalobacter salarius sp. nov. The type strain is strain CG4.1T (=CECT 5903T=LMG 23626T).

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STUDIES OF LIGNIN BIOSYNTHESIS USING ISOTOPIC CARBON: XIII. THE PHENYLPROPANOID SYSTEM IN LIGNIFICATION

Canadian Journal of Biochemistry and Physiology ◽

10.1139/y63-074 ◽

1963 ◽

Vol 41 (1) ◽

pp. 621-628 ◽

Cited By ~ 6

Author(s):

Takayoshi Higuchi ◽

Stewart A. Brown

Keyword(s):

Amino Acids ◽

Ferulic Acid ◽

Cinnamic Acid ◽

Biosynthetic Pathway ◽

Lignin Biosynthesis ◽

Hydroxycinnamic Acid ◽

Coniferyl Alcohol ◽

Phenyllactic Acid ◽

Phenylalanine Deaminase

Techniques of isotope competition and trapping were used to study the phenylpropanoid biosynthetic pathway in lignifying wheat plants. The results in general confirm earlier findings that phenyllactic acid (PLA), p-hydroxyphenyllactic acid (HPLA), phenylpyruvic, cinnamic, caffeic, ferulic, and sinapic acids can participate in lignification. L-Phenylalanine and L-tyrosine were converted to PLA and HPLA, respectively, but there was much less conversion of cinnamic acid to PLA, or p-hydroxycinnamic acid to HPLA. A pathway from phenylalanine to cinnamic acid via PLA, and an analogous pathway involving tyrosine thus remain as possible alternatives to the established routes involving deamination of these amino acids by phenylalanine deaminase or tyrase. Feeding of non-radioactive coniferyl alcohol with ferulic acid-C14 results in the formation of both coniferyl- and sinapyl-type lignin residues having lower specific radioactivities than were obtained after the feeding of ferulic acid-C14 alone. After a 5-hour metabolic period in the presence of ferulic acid-C14, both coniferyl aldehyde and coniferyl alcohol became labelled, and the radioactivity of the aldehyde was much higher than that of the alcohol. There was no evidence of coniferin formation. These findings indicate that coniferyl alcohol is formed from ferulic acid through coniferyl aldehyde, and that coniferin is probably unnecessary for lignification, at least in species other than conifers.

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STUDIES OF LIGNIN BIOSYNTHESIS USING ISOTOPIC CARBON: XIII. THE PHENYLPROPANOID SYSTEM IN LIGNIFICATION

Canadian Journal of Biochemistry and Physiology ◽

10.1139/o63-074 ◽

1963 ◽

Vol 41 (3) ◽

pp. 621-628 ◽

Cited By ~ 23

Author(s):

Takayoshi Higuchi ◽

Stewart A. Brown

Keyword(s):

Amino Acids ◽

Ferulic Acid ◽

Cinnamic Acid ◽

Biosynthetic Pathway ◽

Lignin Biosynthesis ◽

Hydroxycinnamic Acid ◽

Coniferyl Alcohol ◽

Phenyllactic Acid ◽

Phenylalanine Deaminase

Techniques of isotope competition and trapping were used to study the phenylpropanoid biosynthetic pathway in lignifying wheat plants. The results in general confirm earlier findings that phenyllactic acid (PLA), p-hydroxyphenyllactic acid (HPLA), phenylpyruvic, cinnamic, caffeic, ferulic, and sinapic acids can participate in lignification. L-Phenylalanine and L-tyrosine were converted to PLA and HPLA, respectively, but there was much less conversion of cinnamic acid to PLA, or p-hydroxycinnamic acid to HPLA. A pathway from phenylalanine to cinnamic acid via PLA, and an analogous pathway involving tyrosine thus remain as possible alternatives to the established routes involving deamination of these amino acids by phenylalanine deaminase or tyrase. Feeding of non-radioactive coniferyl alcohol with ferulic acid-C14 results in the formation of both coniferyl- and sinapyl-type lignin residues having lower specific radioactivities than were obtained after the feeding of ferulic acid-C14 alone. After a 5-hour metabolic period in the presence of ferulic acid-C14, both coniferyl aldehyde and coniferyl alcohol became labelled, and the radioactivity of the aldehyde was much higher than that of the alcohol. There was no evidence of coniferin formation. These findings indicate that coniferyl alcohol is formed from ferulic acid through coniferyl aldehyde, and that coniferin is probably unnecessary for lignification, at least in species other than conifers.

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