In vivo synthesis of histidine by a cloned histidine ammonia-lyase in Escherichia coli

Fuchs, Roy L.; Kane, James F.

doi:10.1128/jb.162.1.98-101.1985

Cited by 10 publications

(5 citation statements)

References 18 publications

(9 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We usually cultured the cells for 4-8 h to avoid the tracers added to the medium being metabolized and incorporated into thiamin biosynthesized in the cells. However, it has been reported that urocanic acid is transported only slowly in Salmonella tyhpimurium and Klebsiella aerogenes ( 17 ). Therefore we also incubated the cells for 20 h (data not shown), under the same conditions as used by Zeidler; we obtained the same results as after (Fig.…”

Section: Incorporation Of [ 13 C]formate Into the Pyrimidine Moiety Isupporting

confidence: 55%

“…Alternatively, if the permeability of the cell membrane to formamide was inhibited in the presence of urocanic acid, the incorporation of 13 C-formamide would be decreased and it would seem as if incorporation of the label into the pyrimidine moiety were inhibited by urocanic acid. Further, it has been reported that histidine is synthesized from urocanic acid in an Escherichia coli mutant (17). There is a possibility that some of the urocanic acid was converted to histidine, which inhibited the incorporation of [ 13 C]formamide into the pyrimidine moiety in Zeidler's study (14).…”

Section: Incorporation Of L -[ 13 C]histidine Into the Pyrimidine Moimentioning

confidence: 97%

See 1 more Smart Citation

The Direct Precursor of the Pyrimidine Moiety of Thiamin Is Not Urocanic Acid but Histidine in Saccharomyces cerevisiae

Ishida

Tazuya-Murayama

Kijima

et al. 2008

J Nutr Sci Vitaminol

View full text Add to dashboard Cite

The biosynthetic route of the pyrimidine moiety of thiamin is different in prokaryotes and eukaryotes. In prokaryotes, the pyrimidine moiety is synthesized from aminoimidazole ribonucleotide, an intermediate of purine biosynthesis, while in eukaryotes, we have reported that the N-1, C-2, and N-3 atoms of the imidazole ring of histidine are incorporated into N-3, C-4, and the amino group attached to the C-4 atoms of the pyrimidine moiety, respectively, as a unit; the rest of the atoms of the pyrimidine moiety originate from pyridoxine as a unit. It has been reported that urocanic acid, the deaminated compound of histidine, is the direct precursor of the pyrimidine moiety. In the present report, we have investigated whether histidine or urocanic acid is the direct precursor of the pyrimidine moiety in Saccharomyces cerevisiae , using tracer experiments with 1) 13 C-formate and urocanic acid, 2) 15 N-NH 4 Cl and urocanic acid, 3) 15 N-NH 4 Cl and histidine, and 4) 13 C-histidine and urocanic acid. The GC-MS analysis revealed that the incorporation of the 15 N atom of 15 NH 4 Cl was not affected by the presence of urocanic acid, although it was affected by histidine, and the incorporation of 13 C-histidine was not affected by the presence of urocanic acid. These results confirm that histidine is the direct precursor of the pyrimidine moiety of thiamin in S. cerevisiae .

show abstract

Section: Incorporation Of [ 13 C]formate Into the Pyrimidine Moiety Isupporting

confidence: 55%

Section: Incorporation Of L -[ 13 C]histidine Into the Pyrimidine Moimentioning

confidence: 97%

The Direct Precursor of the Pyrimidine Moiety of Thiamin Is Not Urocanic Acid but Histidine in Saccharomyces cerevisiae

Ishida

Tazuya-Murayama

Kijima

et al. 2008

J Nutr Sci Vitaminol

View full text Add to dashboard Cite

show abstract

“…The hutH gene, encoding the cytosolic enzyme HAL, is considered an ancient and basal gene, participating in a core metabolism for the degradation pathway of l -histidine. It distributes broadly in bacteria and promotes them to utilize histidine as carbon and nitrogen sources ( Fuchs and Kane, 1985 ). The loss of the HUT pathway in bacteria only leads to their lack of sufficient capacity for the utilization of histidine, but this is not lethal.…”

Section: Discussionmentioning

confidence: 99%

Origin and Evolution of Enzymes with MIO Prosthetic Group: Microbial Coevolution After the Mass Extinction Event

et al. 2022

View full text Add to dashboard Cite

After major mass extinction events, ancient plants and terrestrial vertebrates were faced with various challenges, especially ultraviolet (UV) light. These stresses probably resulted in changes in the biosynthetic pathways, which employed the MIO (3,5-dihydro-5-methylidene-4H-imidazole-4-one)-dependent enzymes (ammonia-lyase and aminomutase), leading to enhanced accumulation of metabolites for defense against UV radiation, pathogens, and microorganisms. Up to now, the origin and evolution of genes from this superfamily have not been extensively studied. In this report, we perform an analysis of the phylogenetic relations between the members of the aromatic amino acid MIO-dependent enzymes (AAM), which demonstrate that they most probably have a common evolutionary origin from ancient bacteria. In early soil environments, numerous bacterial species with tyrosine ammonia-lyase genes (TAL; EC 4.3.1.23) developed tyrosine aminomutase (TAM; EC 5.4.3.6) activity as a side reaction for competing with their neighbors in the community. These genes also evolved into other TAL-like enzymes, such as histidine ammonia-lyase (HAL, EC 4.3.1.3) and phenylalanine ammonia-lyase (PAL; EC 4.3.1.24), in different bacterial species for metabolite production and accumulation for adaptation to adverse terrestrial environmental conditions. On the other hand, the existence of phenylalanine aminomutase (PAM; EC 5.4.3.10) and phenylalanine/tyrosine ammonia-lyase (PTAL; EC 4.3.1.25) strongly indicates the horizontal gene transfer (HGT) between bacteria, fungi, and plants in symbiotic association after acquiring the PAL gene from their ancestor.

show abstract

“…Media and cultural conditions. Exponential cultures were routinely grown (9) in Luria broth (LB) medium (17), with tetracycline (12.5 p.g/ml) or kanamycin (50 p.g/ml) added for plasmid-containing strains. Cell extracts were prepared as described previously (9) in 50 mM potassium phosphate buffer, pH 6.3 (buffer A), and were used as a source of chitinase.…”

Section: Methodsmentioning

confidence: 99%

Cloning of a Serratia marcescens Gene Encoding Chitinase

Fuchs

McPherson

Drahos

1986

Appl Environ Microbiol

142

View full text Add to dashboard Cite

Serratia marcescens, a chitinase-producing microorganism, was shown to produce five unique chitinolytic proteins with subunit molecular masses of 21, 36, 48, 52, and 57 kilodaltons. A cosmid library of S. marcescens DNA was constructed in the broad-host-range cosmid pLAFRI and screened in Escherichia coli for clones capable of degrading chitin. A total of four independent clones (22to 27-kilobase inserts) were isolated, characterized by restriction endonuclease digestion, and shown to share a common 9.5-kilobase EcoRI fragment apparently encoding the same 57-kilodalton chitinase, the most abundant chitinase produced by S. marcescens. Chitinase expression from these constructs in both E. coli and Pseudomonasfluorescens 701E1 is apparently driven by an S. marcescens promoter. The significantly higher chitinase levels produced in E. coli relative to those in P. fluorescens 701E1 suggest that E. coli may recognize this promoter sequence more efficiently than P. fluorescens. Chitin, a polymer of N-acetylglucosamine (NAG), represents a major structural component of many agronomically important pests including insects, fungi, and nematodes (3, 23). The enzymatic digestion or deformation of the chitin component of these organisms by chitinase could present an effective method for their control. Furthermore, the production and delivery of chitinase to the specific site of infectivity by appropriate rhizoplaneor phyloplane-colonizing bacteria, such as the fluorescent pseudomonads, could present a novel method for biological control. The addition of chitin to soil has been shown to reduce populations of fungal plant pathogens (18) and plant parasitic nematodes (14, 16). Chitin application leads to increased populations of chitinolytic bacteria, especially actinomycetes, and fungi. These increases are correlated with reductions in pathogenic fungi and nematodes and, more importantly, with the reduction of infectivity and, hence, crop damage (6, 14, 23). Although the evidence for the role of chitinase in fungal and nematode control is indirect, the correlation is strong and suggestive. Highly purified chitinase is essential to determine unequivocally its efficacy against fungi and nematodes. More importantly, the gene(s) encoding chitinase must be cloned, expressed, and stably maintained in rhizoplaneor phyloplane-colonizing bacteria to evaluate its in vivo efficacy. Chitinases (EC 3.2.1.14) are a class of hydrolytic enzymes that are commonly found in bacteria, fungi, nematodes, insects, crustaceans, plants, and some vertebrates (21) and that degrade chitin by either an endolytic or exolytic mechanism. Serr(atiai inarcescens was selected as the source of chitinase for the studies described in this paper for the following reasons: (i) crude preparations of chitinases from S. marcescens are commercially available; (ii) an effective affinity chromatographic purification procedure for the S. marcescens chitinases has been reported (19); (iii) the gene(s) encoding these chitinases and their associated regulatory signals is likely ...

show abstract

In vivo synthesis of histidine by a cloned histidine ammonia-lyase in Escherichia coli

Cited by 10 publications

References 18 publications

The Direct Precursor of the Pyrimidine Moiety of Thiamin Is Not Urocanic Acid but Histidine in Saccharomyces cerevisiae

The Direct Precursor of the Pyrimidine Moiety of Thiamin Is Not Urocanic Acid but Histidine in Saccharomyces cerevisiae

Origin and Evolution of Enzymes with MIO Prosthetic Group: Microbial Coevolution After the Mass Extinction Event

Cloning of a Serratia marcescens Gene Encoding Chitinase

Contact Info

Product

Resources

About