Formation of the Nonproteinogenic Amino Acid 2S,3R-Capreomycidine by VioD from the Viomycin Biosynthesis Pathway

ChemBioChem ◽  
2004 ◽  
Vol 5 (9) ◽  
pp. 1278-1281 ◽  
Author(s):  
Xihou Yin ◽  
Kerry L. McPhail ◽  
Kyung-ja Kim ◽  
T. Mark Zabriskie
Keyword(s):  
Amino Acid ◽  
Biosynthesis Pathway

scholarly journals Discovery of a Substrate Selectivity Motif in Amino Acid Decarboxylases Unveils a Taurine Biosynthesis Pathway in Prokaryotes

2013 ◽  
Vol 8 (10) ◽  
pp. 2264-2271 ◽  
Author(s):  
Giulia Agnello ◽  
Leslie L. Chang ◽  
Candice M. Lamb ◽  
George Georgiou ◽  
Everett M. Stone
Keyword(s):  
Amino Acid ◽  
Substrate Selectivity ◽  
Biosynthesis Pathway ◽  
Taurine Biosynthesis

scholarly journals Biosynthesis ofcis,cis-Muconic Acid and Its Aromatic Precursors, Catechol and Protocatechuic Acid, from Renewable Feedstocks by Saccharomyces cerevisiae

2012 ◽  
Vol 78 (23) ◽  
pp. 8421-8430 ◽  
Author(s):  
Christian Weber ◽  
Christine Brückner ◽  
Sheila Weinreb ◽  
Claudia Lehr ◽  
Christine Essl ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Amino Acid ◽  
Adipic Acid ◽  
Aromatic Amino Acid ◽  
Protocatechuic Acid ◽  
Amino Acid Biosynthesis ◽  
Biosynthesis Pathway ◽  
Acid Biosynthesis ◽  
Muconic Acid ◽  
Production Processes

ABSTRACTAdipic acid is a high-value compound used primarily as a precursor for the synthesis of nylon, coatings, and plastics. Today it is produced mainly in chemical processes from petrochemicals like benzene. Because of the strong environmental impact of the production processes and the dependence on fossil resources, biotechnological production processes would provide an interesting alternative. Here we describe the first engineeredSaccharomyces cerevisiaestrain expressing a heterologous biosynthetic pathway converting the intermediate 3-dehydroshikimate of the aromatic amino acid biosynthesis pathway via protocatechuic acid and catechol intocis,cis-muconic acid, which can be chemically dehydrogenated to adipic acid. The pathway consists of three heterologous microbial enzymes, 3-dehydroshikimate dehydratase, protocatechuic acid decarboxylase composed of three different subunits, and catechol 1,2-dioxygenase. For each heterologous reaction step, we analyzed several potential candidates for their expression and activity in yeast to compose a functionalcis,cis-muconic acid synthesis pathway. Carbon flow into the heterologous pathway was optimized by increasing the flux through selected steps of the common aromatic amino acid biosynthesis pathway and by blocking the conversion of 3-dehydroshikimate into shikimate. The recombinant yeast cells finally produced about 1.56 mg/litercis,cis-muconic acid.

scholarly journals Genome-Based Analysis and Gene Dosage Studies Provide New Insight into 3-Hydroxy-4-Methylvalerate Biosynthesis in Ralstonia eutropha

2015 ◽  
Vol 197 (8) ◽  
pp. 1350-1359 ◽  
Author(s):  
Azusa Saika ◽  
Kazunori Ushimaru ◽  
Shoji Mizuno ◽  
Takeharu Tsuge
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Parent Strain ◽  
Ralstonia Eutropha ◽  
Gene Dosage ◽  
Chemical Mutagenesis ◽  
Biosynthesis Pathway ◽  
Content Type ◽  
Carbon Backbone ◽  
Branched Amino Acids

RecombinantRalstonia eutrophastrain PHB−4 expressing the broad-substrate-specificity polyhydroxyalkanoate (PHA) synthase 1 fromPseudomonassp. strain 61-3 (PhaC1Ps) synthesizes a PHA copolymer containing the branched side-chain unit 3-hydroxy-4-methylvalerate (3H4MV), which has a carbon backbone identical to that of leucine. Mutant strain 1F2 was derived fromR. eutrophastrain PHB−4 by chemical mutagenesis and shows higher levels of 3H4MV production than does the parent strain. In this study, to understand the mechanisms underlying the enhanced production of 3H4MV, whole-genome sequencing of strain 1F2 was performed, and the draft genome sequence was compared to that of parent strain PHB−4. This analysis uncovered four point mutations in the 1F2 genome. One point mutation was found in theilvHgene at amino acid position 36 (A36T) of IlvH.ilvHencodes a subunit protein that regulates acetohydroxy acid synthase III (AHAS III). AHAS catalyzes the conversion of pyruvate to 2-acetolactate, which is the first reaction in the biosynthesis of branched amino acids such as leucine and valine. Thus, the A36T IlvH mutation may show AHAS tolerance to feedback inhibition by branched amino acids, thereby increasing carbon flux toward branched amino acid and 3H4MV biosynthesis. Furthermore, a gene dosage study and an isotope tracer study were conducted to investigate the 3H4MV biosynthesis pathway. Based on the observations in these studies, we propose a 3H4MV biosynthesis pathway inR. eutrophathat involves a condensation reaction between isobutyryl coenzyme A (isobutyryl-CoA) and acetyl-CoA to form the 3H4MV carbon backbone.

scholarly journals Diaphorina citri Genome Possesses a Complete Melatonin Biosynthesis Pathway Differentially Expressed under the Influence of the Phytopathogenic Bacterium, Candidatus Liberibacter asiaticus

Insects ◽  
2021 ◽  
Vol 12 (4) ◽  
pp. 317
Author(s):  
Yasser Nehela ◽  
Nabil Killiny
Keyword(s):  
Amino Acid ◽  
Shikimic Acid ◽  
Expression Patterns ◽  
Acid Decarboxylase ◽  
Biosynthesis Pathway ◽  
Diaphorina Citri ◽  
Candidatus Liberibacter Asiaticus ◽  
Phytopathogenic Bacterium ◽  
Candidatus Liberibacter ◽  
Liberibacter Asiaticus

Melatonin is synthesized from the amino acid L-tryptophan via the shikimic acid pathway and ubiquitously distributed in both prokaryotes and eukaryotes. Although most of melatonin biosynthesis genes were characterized in several plants and animal species including the insect model, Drosophila melanogaster, none of these enzymes have been identified from the Asian citrus psyllid, Diaphorina citri. We used comprehensive in silico analysis and gene expression techniques to identify the melatonin biosynthesis-related genes of D. citri and to evaluate the expression patterns of these genes within the adults of D. citri with gradient infection rates (0, 28, 34, 50, 58, and 70%) of the phytopathogenic bacterium Candidatus Liberibacter asiaticus and after the treatment with exogenous melatonin. We showed that the D. citri genome possesses six putative melatonin biosynthesis-related genes including two putative tryptophan 5-hydroxylase (DcT5H-1 and DcT5H-2), a putative aromatic amino acid decarboxylase (DcAADC), two putative arylalkylamine N-acetyltransferase (DcAANAT-1 and DcAANAT-2), and putative N-acetylserotonin O-methyltransferase (DcASMT). The infection with Ca. L. asiaticus decreased the transcript levels of all predicted genes in the adults of D. citri. Moreover, melatonin supplementation induced their expression levels in both healthy and Ca. L. asiaticus-infected psyllids. These findings confirm the association of these genes with the melatonin biosynthesis pathway.

scholarly journals Cloning and characterization of cobA, one of vitamin B12 biosynthesis pathway genes from Selenomonas ruminantium

2021 ◽  
Vol 10 (2) ◽  
pp. 131-135
Author(s):  
Lívia Fecskeová ◽  
Peter Pristaš ◽  
Peter Javorský
Keyword(s):  
Amino Acid ◽  
Vitamin B12 ◽  
Biosynthetic Pathway ◽  
Anaerobic Bacteria ◽  
Protein Sequences ◽  
Synthesis Process ◽  
Biosynthesis Pathway ◽  
Selenomonas Ruminantium ◽  
Main Producer

Bacterial biosynthesis of vitamin B12 can occur via either aerobic or anaerobic route. While the aerobic pathway has been fully elucidated and understood, less is known about the anaerobic pathway. Selenomonas ruminantium is thought to be the main producer of this vitamin in rumen environment and must use the anaerobic pathway. In our work we found one of the genes of vitamin B12 biosynthetic pathway of S. ruminantium, encoding for the cobalamin adenosyltransferase, enzyme taking part at the last steps of the synthesis process. Deduced amino acid sequence showed the highest similarity to cobalamin adenosyltransferases of other ruminal anaerobic bacteria and that of species Selenomonas. Phylogenetic comparisons of CobA protein sequences of several anaerobic bacteria of Clostridiale order indicate possible horizontal transfer of this gene.

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