scholarly journals Characterization of an l-Ascorbate Catabolic Pathway with Unprecedented Enzymatic Transformations

2020 ◽  
Vol 142 (4) ◽  
pp. 1657-1661 ◽  
Author(s):  
Tyler M. M. Stack ◽  
Katelyn N. Morrison ◽  
Thomas M. Dettmer ◽  
Brendan Wille ◽  
Chan Kim ◽  
...  
Keyword(s):  
Catabolic Pathway

scholarly journals A Pathway for Degradation of Uracil to Acetyl Coenzyme A in Bacillus megaterium

2020 ◽  
Vol 86 (7) ◽  
Author(s):  
Di Zhu ◽  
Yifeng Wei ◽  
Jinyu Yin ◽  
Dazhi Liu ◽  
Ee Lui Ang ◽  
...  
Keyword(s):  
Energy Source ◽  
Bacillus Megaterium ◽  
Coenzyme A ◽  
Catabolic Pathway ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Content Type ◽  
Biochemical Pathways ◽  
Acetyl Coenzyme

ABSTRACT Bacteria utilize diverse biochemical pathways for the degradation of the pyrimidine ring. The function of the pathways studied to date has been the release of nitrogen for assimilation. The most widespread of these pathways is the reductive pyrimidine catabolic pathway, which converts uracil into ammonia, carbon dioxide, and β-alanine. Here, we report the characterization of a β-alanine:pyruvate aminotransferase (PydD2) and an NAD+-dependent malonic semialdehyde dehydrogenase (MSDH) from a reductive pyrimidine catabolism gene cluster in Bacillus megaterium. Together, these enzymes convert β-alanine into acetyl coenzyme A (acetyl-CoA), a key intermediate in carbon and energy metabolism. We demonstrate the growth of B. megaterium in defined medium with uracil as its sole carbon and energy source. Homologs of PydD2 and MSDH are found in association with reductive pyrimidine pathway genes in many Gram-positive bacteria in the order Bacillales. Our study provides a basis for further investigations of the utilization of pyrimidines as a carbon and energy source by bacteria. IMPORTANCE Pyrimidine has wide occurrence in natural environments, where bacteria use it as a nitrogen and carbon source for growth. Detailed biochemical pathways have been investigated with focus mainly on nitrogen assimilation in the past decades. Here, we report the discovery and characterization of two important enzymes, PydD2 and MSDH, which constitute an extension for the reductive pyrimidine catabolic pathway. These two enzymes, prevalent in Bacillales based on our bioinformatics studies, allow stepwise conversion of β-alanine, a previous “end product” of the reductive pyrimidine degradation pathway, to acetyl-CoA as carbon and energy source.

Characterization of styrene catabolic pathway in Pseudomonas fluorescens ST

2004 ◽  
Vol 54 (2-3) ◽  
pp. 183-187 ◽  
Author(s):  
Giuseppina Bestetti ◽  
Patrizia Di Gennaro ◽  
Andrea Colmegna ◽  
Ilaria Ronco ◽  
Enrica Galli ◽  
...  
Keyword(s):  
Pseudomonas Fluorescens ◽  
Catabolic Pathway

scholarly journals Expression and Characterization of Phenacetaldehyde Dehydrogenase from the Styrene Catabolic Pathway

2006 ◽  
Vol 20 (4) ◽  
Author(s):  
Maryam Naseri‐Jabari ◽  
Shahram Emami ◽  
George Gassner
Keyword(s):  
Catabolic Pathway

scholarly journals Molecular characterization of the Pseudomonas putida 2,3-butanediol catabolic pathway

1994 ◽  
Vol 124 (2) ◽  
pp. 141-150 ◽  
Author(s):  
Min Huang ◽  
Fred Bernd Oppermann ◽  
Alexander Steinbüchel
Keyword(s):  
Pseudomonas Putida ◽  
Molecular Characterization ◽  
Catabolic Pathway

scholarly journals Characterization of the β-Ketoadipate Pathway in Sinorhizobium meliloti

2006 ◽  
Vol 72 (8) ◽  
pp. 5403-5413 ◽  
Author(s):  
Allyson M. MacLean ◽  
Gordon MacPherson ◽  
Punita Aneja ◽  
Turlough M. Finan
Keyword(s):  
Aromatic Compounds ◽  
Related Species ◽  
Sinorhizobium Meliloti ◽  
Transcriptional Regulator ◽  
Transferase Activity ◽  
Catabolic Pathway ◽  
Closely Related Species ◽  
Coa Transferase ◽  
Transcriptional Units

ABSTRACT Aromatic compounds represent an important source of energy for soil-dwelling organisms. The β-ketoadipate pathway is a key metabolic pathway involved in the catabolism of the aromatic compounds protocatechuate and catechol, and here we show through enzymatic analysis and mutant analysis that genes required for growth and catabolism of protocatechuate in the soil-dwelling bacterium Sinorhizobium meliloti are organized on the pSymB megaplasmid in two transcriptional units designated pcaDCHGB and pcaIJF. The pcaD promoter was mapped by primer extension, and expression from this promoter is demonstrated to be regulated by the LysR-type protein PcaQ. β-Ketoadipate succinyl-coenzyme A (CoA) transferase activity in S. meliloti was shown to be encoded by SMb20587 and SMb20588, and these genes have been renamed pcaI and pcaJ, respectively. These genes are organized in an operon with a putative β-ketoadipyl-CoA thiolase gene (pcaF), and expression of the pcaIJF operon is shown to be regulated by an IclR-type transcriptional regulator, SMb20586, which we have named pcaR. We show that pcaR transcription is negatively autoregulated and that PcaR is a positive regulator of pcaIJF expression and is required for growth of S. meliloti on protocatechuate as the carbon source. The characterization of the protocatechuate catabolic pathway in S. meliloti offers an opportunity for comparison with related species, including Agrobacterium tumefaciens. Differences observed between S. meliloti and A. tumefaciens pcaIJ offer the first evidence of pca genes that may have been acquired after speciation in these closely related species.

Characterization of the catabolic pathway for a phenylcoumaran-type lignin-derived biaryl in Sphingobium sp. strain SYK-6

2014 ◽  
Vol 25 (5) ◽  
pp. 735-745 ◽  
Author(s):  
Kenji Takahashi ◽  
Naofumi Kamimura ◽  
Shojiro Hishiyama ◽  
Hirofumi Hara ◽  
Daisuke Kasai ◽  
...  
Keyword(s):  
Catabolic Pathway

scholarly journals Identification and Functional Characterization of Sphingomonas macrogolitabida Strain TFA Genes Involved in the First Two Steps of the Tetralin Catabolic Pathway

2003 ◽  
Vol 185 (6) ◽  
pp. 2026-2030 ◽  
Author(s):  
Emilia Moreno-Ruiz ◽  
María José Hernáez ◽  
Olga Martínez-Pérez ◽  
Eduardo Santero
Keyword(s):  
Functional Characterization ◽  
Catabolic Pathway ◽  
Biodegradation Pathway ◽  
Dioxygenase Activity

ABSTRACT Five genes involved in the two initial steps of the tetralin biodegradation pathway of Sphingomonas macrogolitabida strain TFA have been characterized. ThnA1A2 and ThnA3A4, components of the ring-hydroxylating dioxygenase, were encoded in divergently transcribed operons. ThnA1, ThnA2, and ThnA3 were essential for tetralin ring-hydroxylating dioxygenase activity. ThnB was identified as a dehydrogenase required for tetralin biodegradation.

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