Purification and Properties of Histidinol Dehydrogenase from Escherichia coli B

Andorn, N.; Aronovitch, J.

doi:10.1099/00221287-128-3-579

Cited by 5 publications

(4 citation statements)

References 7 publications

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“…The actual pH value of the reaction mixture containing the crude enzyme solution of liver and the buffer solution (pH 11.0) was 9.5, when determined later. This optimum pH value was almost similar to those observed in general microorganisms (9.5) (Andorn and Aronovitch, 1982) and plants (9.2) (Nagai and Scheidegger, 1991). However, since pH values usually tended to be expressed with those of buffer solution used, we reported in the first paper (Wadud et al 2001b) that the optimum pH values of HLDase were 11.0 in cattle liver and 9.0 in cattle kidney.…”

Section: Histidinol Dehydrogenase In Ruminantssupporting

confidence: 84%

“…Incidentally, our recent results demonstrated that not only rumen protozoa but also rumen bacteria collected from goats fed haycube and concentrate could not synthesize histidine from histidinol which had been known as a precursor at the final step of the pathway for de novo biosynthesis of histidine in general microorganisms (Andorn and Aronovitch, 1982) and plants (Nagai and Scheidegger, 1991). As shown in Table 3, histidinol, imidazolepyruvate, imidazoleacetate and imidazolelactate were used as substrates in this study, and histidinol and imidazolelactate remained unchanged even after 18 h incubation, although the values shown in Table 3 were those only after 12 h incubation.…”

Section: Historical Backgroundmentioning

confidence: 94%

“…Nowadays histidine has been recognized as an essential amino acid for human adults (Metges et al, 1999). One mysterious thing is that in spite of the long-term argument with regard to the essentiality of histidine for human adults, there have been no reports on the activity of histidinol dehydrogenase in animal tissues which had already been revealed in microorganisms (Andorn and Aronovitch, 1982) and plants (Nagai and Scheidegger, 1991), although incorporations of 15 N from 15 NH 4 Cl and 15 N-urea in human adults and 14 C from H 14 COOH into histidine in human fetal liver (Levy and Coon, 1952) were examined. The paper by Kotb and Wixom (1971) was the only report in which histidinol was used.…”

Section: Human Beingsmentioning

confidence: 99%

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Essentiality of Histidine in Ruminant and Other Animals Including Human Beings

Onodera¹

2003

Asian Australas. J. Anim. Sci

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Concept and establishment of essential amino acids in animals and human beings rendered immeasurable contributions to animal production and human health. In ruminant animals, however, essential amino acids have never been completely established. The present review proposes a hypothesis that histidine may not be an essential amino acid for normal growing cattle (Japanese black) at least at the growing stage after about 450 kg of body weight on the basis of the experimental results of histidinol dehydrogenase activities in some tissues of the cattle together with hints from which the hypothesis was derived. At the same time, histidinol dehydrogenase activities in liver, kidney and muscle of swine, mouse, fowl and wild duck will be shown and the essentiality of histidine in these animals will be discussed. Finally, the essentiality of histidine for adult human will briefly be discussed.

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Section: Histidinol Dehydrogenase In Ruminantssupporting

confidence: 84%

Section: Historical Backgroundmentioning

confidence: 94%

Section: Human Beingsmentioning

confidence: 99%

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Essentiality of Histidine in Ruminant and Other Animals Including Human Beings

Onodera¹

2003

Asian Australas. J. Anim. Sci

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“…These genes encode the protein product of histidinol dehydrogenase and ATP phosphoribosyltransferase, respectively, and were among the DEGs that were more highly expressed. However, other studies have reported that the presence of urea inhibits the activities of these enzymes (Yourno, 1968;Andorn and Aronovitch, 1982;Senior, 1989;Mizukami et al, 1994).…”

Section: Discussionmentioning

confidence: 94%

Complete Genome Sequencing and Transcriptome Analysis of Nitrogen Metabolism of Succinivibrio dextrinosolvens Strain Z6 Isolated From Dairy Cow Rumen

2020

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The unclassified Succinivibrionaceae lineages are abundant in high yielding multiparous cows, and their presence is positively correlated with milk yield and fat percentage and reduces methane emissions. However, it is still unclear which species are associated with the most efficient feed nutrient utilization and productivity. Here, we used integrated whole genome sequencing and matrix-assisted laser desorption/ionization mass spectrometry, coupled with phenotypic and chemotaxonomic analysis, to characterize S. dextrinosolvens Z6, a species in Succinivibrionaceae isolated from the rumen. To assess the role of S. dextrinosolvens Z6 in nitrogen metabolism, cells grown in different nitrogen sources were analyzed by RNA sequencing. The whole genome sequence result revealed a genome size of 3.47 Mbp with 38.9% of G + C content. A total of 2993 encoding sequences account for 98%. The genes for regulating carbohydrate (10.6%) and amino acid (9%) transport and metabolism were the most abundant. ANI (Average nucleotide identity) showed that SD-Z6 was most closely related to SD-22B (99.96%). The whole genome alignment of SD-Z6 with SD-22B showed a more than 0.34 Mb nucleotide difference. Growth of SD-Z6 occurred at a temperature 36-42 • C with an optimum at 39.7 • C, pH 6-8; the optimum pH was 6.9 and with 0-1% (w/v) NaCl. The maximum growth (OD 600 0.825 ± 0.12) and microbial crude protein (MCP) (178.2 µg/ml) were observed in cells grown in amino acid. The maximum concentration of ammonia (3.96 ± 1.2) was observed in urea containing media and 1.06 mM (26.7% of the produced) remained after 24 h incubation. Activities of urease and glutamine synthase (P < 0.01) and glutamate dehydrogenase (P < 0.05) were significantly different in nitrogen and growth phase. Glutamate synthetase (P < 0.01) was significantly different only at different growth phases. In total, 1246 differentially expressed genes (DEGs) were identified in all nitrogen. Among DEGs, 33 were related to nitrogen metabolism. Their expression correlated with nitrogen sources and the intensity of enzyme activity. This result enhances our understanding of the roles of Succinivibrionaceae in the efficient nitrogen utilization and on environmental protection.

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Studies on the possibility of histidine biosynthesis from histidinol, imidazolepyruvic acid, imidazoleacetic acid, and imidazolelactic acid by mixed ruminal bacteria, protozoa, and their mixture in vitro

Wadud

Onodera

2001

Applied Microbiology and Biotechnology

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The possibility of histidine (His) synthesis using a main biosynthetic pathway involving histidinol (HDL) and also the recycling capability of imidazolic compounds such as imidazolepyruvic acid (ImPA), imidazoleacetic acid (ImAA), and imidazolelactic acid (ImLA) to produce His were investigated using mixed ruminal bacteria (B), protozoa (P), and a mixture of both (BP) in an in vitro system. Rumen microorganisms were anaerobically incubated at 39 degrees C for 18 h with or without each substrate (2 mM) mentioned. His and other related compounds produced in both the supernatants and hydrolyzates of the incubation were analyzed by high-performance liquid chromatography. B, P, and BP suspensions failed to show His synthesizing ability when incubated with HDL. His was synthesized from ImPA by B, P, and BP. Expressed in units "per gram of microbial nitrogen (MN)", ImPA disappearance was greatest in B (72.7 micromol/g MN per hour), followed by BP (33.13 micromol/g MN per hour) and then P (18.6 micromol/g MN per hour) for the 18-h incubation period. The production of His from ImPA in B (240.0, 275.9, and 261.2 micromol/g MN in 6, 12, and 18 h incubation, respectively) was about 3.5 times higher than that in P (67.3, 83.8, and 72.7 micromol/g MN in 6, 12, and 18 h incubation, respectively). Other metabolites produced from ImPA were ImLA, ImAA, histamine (HTM), and urocanic acid (URA), found in all microbial suspensions. ImLA as a substrate remained without diminution in all microbial suspensions. Although ImAA was found to be degraded to a small extent (3.4-6.3%) only after 18 h incubation, neither His nor other metabolites were detected on the chromatograms. These results have been demonstrated for the first time in rumen microorganisms and suggest that His may be an essential amino acid for rumen microorganisms.

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Purification and Properties of Histidinol Dehydrogenase from Escherichia coli B

Cited by 5 publications

References 7 publications

Essentiality of Histidine in Ruminant and Other Animals Including Human Beings

Essentiality of Histidine in Ruminant and Other Animals Including Human Beings

Complete Genome Sequencing and Transcriptome Analysis of Nitrogen Metabolism of Succinivibrio dextrinosolvens Strain Z6 Isolated From Dairy Cow Rumen

Studies on the possibility of histidine biosynthesis from histidinol, imidazolepyruvic acid, imidazoleacetic acid, and imidazolelactic acid by mixed ruminal bacteria, protozoa, and their mixture in vitro

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