Proline production via the arginine biosynthetic pathway: transfer of regulatory mutations of arginine biosynthesis into a proline-producing strain ofSerratia marcescens

1986 ◽  
Vol 24 (2) ◽  
pp. 153-158 ◽  
Author(s):  
Masaki Sugiura ◽  
Shin-ichi Suzuki ◽  
Tsutomu Takagi ◽  
Masahiko Kisumi
Keyword(s):  
Biosynthetic Pathway ◽  
Arginine Biosynthesis ◽  
Regulatory Mutations

scholarly journals Surprising Arginine Biosynthesis: a Reappraisal of the Enzymology and Evolution of the Pathway in Microorganisms

2007 ◽  
Vol 71 (1) ◽  
pp. 36-47 ◽  
Author(s):  
Ying Xu ◽  
Bernard Labedan ◽  
Nicolas Glansdorff
Keyword(s):  
Biosynthetic Pathway ◽  
De Novo ◽  
Single Gene ◽  
Metabolic Function ◽  
Gene Products ◽  
Arginine Biosynthesis ◽  
Acetyl Coenzyme A ◽  
Bacterial Phyla ◽  
Acetyl Group ◽  
Acetylglutamate Synthase

SUMMARY Major aspects of the pathway of de novo arginine biosynthesis via acetylated intermediates in microorganisms must be revised in light of recent enzymatic and genomic investigations. The enzyme N-acetylglutamate synthase (NAGS), which used to be considered responsible for the first committed step of the pathway, is present in a limited number of bacterial phyla only and is absent from Archaea. In many Bacteria, shorter proteins related to the Gcn5-related N-acetyltransferase family appear to acetylate l-glutamate; some are clearly similar to the C-terminal, acetyl-coenzyme A (CoA) binding domain of classical NAGS, while others are more distantly related. Short NAGSs can be single gene products, as in Mycobacterium spp. and Thermus spp., or fused to the enzyme catalyzing the last step of the pathway (argininosuccinase), as in members of the Alteromonas-Vibrio group. How these proteins bind glutamate remains to be determined. In some Bacteria, a bifunctional ornithine acetyltransferase (i.e., using both acetylornithine and acetyl-CoA as donors of the acetyl group) accounts for glutamate acetylation. In many Archaea, the enzyme responsible for glutamate acetylation remains elusive, but possible connections with a novel lysine biosynthetic pathway arose recently from genomic investigations. In some Proteobacteria (notably Xanthomonadaceae) and Bacteroidetes, the carbamoylation step of the pathway appears to involve N-acetylornithine or N-succinylornithine rather than ornithine. The product N-acetylcitrulline is deacetylated by an enzyme that is also involved in the provision of ornithine from acetylornithine; this is an important metabolic function, as ornithine itself can become essential as a source of other metabolites. This review insists on the biochemical and evolutionary implications of these findings.

scholarly journals Evolution of Arginine Biosynthesis in the Bacterial Domain: Novel Gene-Enzyme Relationships from Psychrophilic Moritella Strains (Vibrionaceae) and Evolutionary Significance of N-α-Acetyl Ornithinase

2000 ◽  
Vol 182 (6) ◽  
pp. 1609-1615 ◽  
Author(s):  
Ying Xu ◽  
Ziyuan Liang ◽  
Christianne Legrain ◽  
Hans J. Rüger ◽  
Nicolas Glansdorff
Keyword(s):  
Biosynthetic Pathway ◽  
Evolutionary Significance ◽  
Arginine Biosynthesis ◽  
Gene Encoding ◽  
Cold Adapted ◽  
Continuous Sequence ◽  
Cold Active ◽  
Acetyl Group ◽  
Clustering Pattern ◽  
Bacterial Domain

ABSTRACT In the arginine biosynthetic pathway of the vast majority of prokaryotes, the formation of ornithine is catalyzed by an enzyme transferring the acetyl group of N-α-acetylornithine to glutamate (ornithine acetyltransferase [OATase]) (argJencoded). Only two exceptions had been reported—theEnterobacteriaceae and Myxococcus xanthus(members of the γ and δ groups of the classProteobacteria, respectively)—in which ornithine is produced from N-α-acetylornithine by a deacylase, acetylornithinase (AOase) (argE encoded). We have investigated the gene-enzyme relationship in the arginine regulons of two psychrophilic Moritella strains belonging to theVibrionaceae, a family phylogenetically related to theEnterobacteriaceae. Most of the arg genes were found to be clustered in one continuous sequence divergently transcribed in two wings, argE and argCBFGH(A)[“H(A)” indicates that the argininosuccinase gene consists of a part homologous to known argH sequences and of a 3′ extension able to complement an Escherichia colimutant deficient in the argA gene, encodingN-α-acetylglutamate synthetase, the first enzyme committed to the pathway]. Phylogenetic evidence suggests that this new clustering pattern arose in an ancestor common toVibrionaceae and Enterobacteriaceae, where OATase was lost and replaced by a deacylase. The AOase and ornithine carbamoyltransferase of these psychrophilic strains both display distinctly cold-adapted activity profiles, providing the first cold-active examples of such enzymes.

Arginine biosynthesis in Legionella pneumophila: absence of N-acetylglutamate synthetase

1983 ◽  
Vol 29 (9) ◽  
pp. 1230-1233 ◽  
Author(s):  
Martha J. Tesh ◽  
Richard D. Miller
Keyword(s):  
Legionella Pneumophila ◽  
Biosynthetic Pathway ◽  
Defined Medium ◽  
Chemically Defined Medium ◽  
Arginine Biosynthesis ◽  
Cell Extracts

Legionella pneumophila was unable to grow in a chemically defined medium without arginine because it could not carry out the first step in the biosynthetic pathway, the conversion of glutamate to N-acetylglutamate. All strains examined could grow when N-acetylglutamate (or other later arginine precursors) were substituted for arginine. No activity corresponding to N-acetylglutamate synthetase could be detected in cell extracts of L. pneumophila.

Hypoxia inhibits L-arginine synthesis from L-citrulline in porcine pulmonary artery endothelial cells

1995 ◽  
Vol 269 (5) ◽  
pp. L581-L587 ◽  
Author(s):  
Y. Su ◽  
E. R. Block
Keyword(s):  
Endothelial Cells ◽  
Pulmonary Artery ◽  
Biosynthetic Pathway ◽  
Argininosuccinate Synthetase ◽  
Argininosuccinate Lyase ◽  
Arginine Biosynthesis ◽  
Intact Cells ◽  
Porcine Pulmonary Artery

Both non-arginine-depleted and arginine-depleted pulmonary artery endothelial cells (PAEC) actively convert citrulline into arginine. Exposure to hypoxia for 4-24 h inhibited arginine synthesis from citrulline in intact cells and in cell homogenates. The conversion of L-citrulline to L-argininosuccinate by argininosuccinate synthetase (AS) was inhibited by exposure to hypoxia for 4, 12, or 24 h. The conversion of argininosuccinate to arginine by argininosuccinate lyase was inhibited by exposure to hypoxia for 24 h but not for 4-12 h. The decrease of L-arginine biosynthesis during hypoxia coincided with the increase of intracellular glutamine content and was abrogated by preventing an increase in intracellular glutamine. In addition, AS activity was inversely related to glutamine content in the medium. These results indicate that hypoxia inhibited the L-arginine biosynthetic pathway via decreased activity of AS. The latter is related to increased glutamine content. Hypoxic inhibition of arginine synthesis from citrulline did not result in a decrease of arginine content, suggesting that PAEC are able to maintain intracellular arginine for up to 24 h despite reduction in the L-arginine biosynthetic pathway.

scholarly journals SALT STRESS INHIBITS ARGININE BIOSYNTHESIS IN TEPARY BEAN (PHASEOLUSA CUTIFOLIUS)

HortScience ◽  
1990 ◽  
Vol 25 (9) ◽  
pp. 1091a-1091
Author(s):  
Ignacio Lazcano-Ferrat ◽  
Carol J. Lovatt
Keyword(s):  
Salt Stress ◽  
Biosynthetic Pathway ◽  
Molar Ratio ◽  
Agricultural Experiment Station ◽  
Arginine Biosynthesis ◽  
Tepary Bean ◽  
Salt Treatment ◽  
Agricultural Experiment ◽  
The University ◽  
Carbamylphosphate Synthetase

Two lines of tepary bean, PI 321-638 and PI 319-443, were salinized at age 7 days with Shive's nutrient solution plus 60 mM NaCl-CaCl2 in a 2:1 molar ratio. Salt was added at the rate of 1/3 the final concentration every other day. The osmotic potential of the salinizing solution was -0.33 MPa. Fifteen days of salt treatment reduced plant growth 45% and inhibited the incorporation of NaH14CO3 into the combined pool of arginine plus urea 60 and 85% for the two lines, respectively. The salt sensitive step in the arginine biosynthetic pathway was identified as carbamylphosphate synthetase in both lines, Incorporation of [14C]citrulline and [14C]carbamylphosphate plus ornithine were not inhibited by the salt treatment, but the incorporation of NaH14CO3 remained inhibited even in the presence of added ornithine (10 mM). Inhibition at carbamylphosphate synthetase was confirmed by demonstration that the incorporation of NaH14CO3 into UMP was also inhibited by salt stress. Evidence is provided suggesting that reduced availability of ornithine additionally compromised both arginine and pyrimidine biosynthesis during salt stress.Supported by the Citrus Research Center and Agricultural Experiment Station of the University of California, Riverside.

scholarly journals A Fragment-based approach to assess the ligandability of ArgB, ArgC, ArgD and ArgF in the L-arginine biosynthetic pathway of Mycobacterium tuberculosis

2021 ◽  
Author(s):  
Pooja Gupta ◽  
Sherine E. Thomas ◽  
James Cory-Wright ◽  
Víctor Sebastián-Pérez ◽  
Ailidh Burgess ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Drug Discovery ◽  
Animal Models ◽  
Biosynthetic Pathway ◽  
Crystallographic Data ◽  
Biosynthesis Pathway ◽  
Arginine Biosynthesis ◽  
X Ray ◽  
Chemical Inhibition ◽  
Target Activity

AbstractThe L-arginine biosynthesis pathway consists of eight enzymes that catalyse the conversion of L-glutamate to L-arginine, appears to be attractive target for anti-Tuberculosis (TB) drug discovery. Starvation of M. tuberculosis deleted for either argB or argF genes led to rapid sterilization of these strains in mice while Chemical inhibition of ArgJ with Pranlukast was also found to clear chronic M. tuberculosis infection in animal models. In this work, the ligandability of four enzymes of the pathway ArgB, ArgC, ArgD and ArgF is explored using a fragment-based approach. We reveal several hits for these enzymes validated with biochemical and biophysical assays, and X-ray crystallographic data, which in the case of ArgB were further confirmed to have on-target activity against M. tuberculosis. These results demonstrate the potential of more enzymes in this pathway to be targeted with dedicated drug discovery programmes.

New insights into heparan sulphate biosynthesis from the study of mutant mice

2002 ◽  
Vol 69 ◽  
pp. 47-57 ◽  
Author(s):  
Catherine L. R. Merry ◽  
John T. Gallagher
Keyword(s):  
Growth Factors ◽  
Biosynthetic Pathway ◽  
Heparan Sulphate ◽  
Mutant Mice ◽  
Gene Products ◽  
Multiple Gene ◽  
Adhesion Proteins ◽  
Ligand Interactions

Heparan sulphate (HS) is an essential co-receptor for a number of growth factors, morphogens and adhesion proteins. The biosynthetic modifications involved in the generation of a mature HS chain may determine the strength and outcome of HS–ligand interactions. These modifications are catalysed by a complex family of enzymes, some of which occur as multiple gene products. Various mutant mice have now been generated, which lack the function of isolated components of the HS biosynthetic pathway. In this discussion, we outline the key findings of these studies, and use them to put into context our own work concerning the structure of the HS generated by the Hs2st-/- mice.

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