Excretion of an acid semialdehyde by Gloeomonas

1971 ◽  
Vol 10 (5) ◽  
pp. 967-976 ◽  
Author(s):  
S.S. Badour ◽  
E.R. Waygood
Keyword(s):  
Acid Semialdehyde

scholarly journals Identification and Validation of Aspartic Acid Semialdehyde Dehydrogenase as a New Anti-Mycobacterium Tuberculosis Target

2015 ◽  
Vol 16 (10) ◽  
pp. 23572-23586 ◽  
Author(s):  
Jianzhou Meng ◽  
Yanhui Yang ◽  
Chunling Xiao ◽  
Yan Guan ◽  
Xueqin Hao ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Aspartic Acid ◽  
Semialdehyde Dehydrogenase ◽  
Acid Semialdehyde

Oxidative Ring-Cleavage of Catechol in meta-Position by Superoxide

1989 ◽  
Vol 44 (3-4) ◽  
pp. 207-211 ◽  
Author(s):  
Rudolf Müller ◽  
Franz Lingens
Keyword(s):  
Spectroscopic Data ◽  
Mass Spectra ◽  
Room Temperature ◽  
Picolinic Acid ◽  
Uv Spectra ◽  
Cleavage Product ◽  
Ring Cleavage ◽  
Meta Position ◽  
Acid Semialdehyde ◽  
Yellow Compound

Abstract Superoxide reacts with catechol in dimethylsulfoxide to form a yellow product. The structure of this product was established by different methods. UV-spectra of the yellow compound corresponded under all circumstances to those of enzymatically produced 2-hydroxymuconic acid semialdehyde. In the presence of ammonia the product was converted to picolinic acid. The UV - spectra, the retention times in GC and HPLC and the mass spectra after methylation corresponded to those of authentic picolinic acid. Thus, the yellow reaction product was unequivocally identified as 2-hydroxymuconic acid semialdehyde. The formation of the me/a-cleavage product was only observed at low catechol concentrations (<2 mM) , at higher concentrations the product was not formed. The reaction was complete within 10 min at room temperature. Spectroscopic data suggest a first intermediate in the reaction with λmax = 804 nm, 772 nm and 660 nm.

Data on obtention and neurotropic activity of succinic acid semialdehyde

1969 ◽  
Vol 3 (12) ◽  
pp. 697-700 ◽  
Author(s):  
R. U. Ostrovskaya ◽  
N. M. Tsybina ◽  
T. V. Protopopova ◽  
A. P. Skoldinov
Keyword(s):  
Succinic Acid ◽  
Neurotropic Activity ◽  
Acid Semialdehyde

scholarly journals Degradation of 1,3-Dichloropropene by Pseudomonas cichorii 170

1998 ◽  
Vol 64 (8) ◽  
pp. 2931-2936 ◽  
Author(s):  
Gerrit J. Poelarends ◽  
Marga Wilkens ◽  
Michael J. Larkin ◽  
Jan Dirk van Elsas ◽  
Dick B. Janssen
Keyword(s):  
Pcr Analysis ◽  
Rhodococcus Rhodochrous ◽  
Negative Bacterium ◽  
Haloalkane Dehalogenase ◽  
Positive Bacterium ◽  
Pseudomonas Cichorii ◽  
Low Concentrations ◽  
Suicide Substrate ◽  
Chloroacrylic Acid Dehalogenase ◽  
Acid Semialdehyde

ABSTRACT The gram-negative bacterium Pseudomonas cichorii 170, isolated from soil that was repeatedly treated with the nematocide 1,3-dichloropropene, could utilize low concentrations of 1,3-dichloropropene as a sole carbon and energy source. Strain 170 was also able to grow on 3-chloroallyl alcohol, 3-chloroacrylic acid, and several 1-halo-n-alkanes. This organism produced at least three different dehalogenases: a hydrolytic haloalkane dehalogenase specific for haloalkanes and two 3-chloroacrylic acid dehalogenases, one specific for cis-3-chloroacrylic acid and the other specific for trans-3-chloroacrylic acid. The haloalkane dehalogenase and thetrans-3-chloroacrylic acid dehalogenase were expressed constitutively, whereas the cis-3-chloroacrylic acid dehalogenase was inducible. The presence of these enzymes indicates that 1,3-dichloropropene is hydrolyzed to 3-chloroallyl alcohol, which is oxidized in two steps to 3-chloroacrylic acid. The latter compound is then dehalogenated, probably forming malonic acid semialdehyde. The haloalkane dehalogenase gene, which is involved in the conversion of 1,3-dichloropropene to 3-chloroallyl alcohol, was cloned and sequenced, and this gene turned out to be identical to the previously studieddhaA gene of the gram-positive bacterium Rhodococcus rhodochrous NCIMB13064. Mutants resistant to the suicide substrate 1,2-dibromoethane lacked haloalkane dehalogenase activity and therefore could not utilize haloalkanes for growth. PCR analysis showed that these mutants had lost at least part of the dhaA gene.

scholarly journals Expression of a Pseudomonas putidaAminotransferase Involved in Lysine Catabolism Is Induced in the Rhizosphere

2001 ◽  
Vol 67 (11) ◽  
pp. 5219-5224 ◽  
Author(s):  
Manuel Espinosa-Urgel ◽  
Juan-Luis Ramos
Keyword(s):  
Amino Acid ◽  
Glutaric Acid ◽  
Insertional Mutagenesis ◽  
Carbon Sources ◽  
Aminotransferase Activity ◽  
Transcriptional Fusion ◽  
Direct Genetic Evidence ◽  
Acid Semialdehyde ◽  
Transcriptional Fusions ◽  
Lysine Catabolism

ABSTRACT Using a transposon carrying a promoterless luxoperon to generate transcriptional fusions by insertional mutagenesis, we have identified a Pseudomonas putida gene with increased expression in the presence of corn root exudates. Expression of the transcriptional fusion, induced by the amino acid lysine, was detected in P. putida in the rhizosphere of plants as well as in response to seed exudates. The mutant was unable to grow on lysine or δ-aminovalerate as carbon sources, which indicates that the affected function is involved in the pathway for lysine catabolism. However, the mutant strain grew with glutaric acid, the product of δ-aminovalerate metabolism via glutaric acid semialdehyde, as a C source. The translated sequence of the interrupted gene showed high levels of similarity with aminotransferases. These sets of data suggest that the product of this gene has δ-aminovalerate aminotransferase activity. This is the first direct genetic evidence correlating a DNA sequence with such activity inPseudomonadaceae.

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