STUDIES ON LYSINE FERMENTATION III. Α, Ε-Diaminopimelic ACID ACCUMULATION AND DIAMINOPIMELIC ACID DECARBOXYLASE

Nakayama, Kiyoshi; Kinoshita, Shukuo

doi:10.2323/jgam.7.161

Cited by 5 publications

(4 citation statements)

References 5 publications

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“…The phenomenon of lysine inhibition of diaminopimelate decarboxylase reported in this paper agrees with the observations of others (11,12,21,34); however, the earlier studies employed 10 to 40 mM lysine, considerably greater than the inhibitor concentrations utilized in this research and an order of magnitude higher than physiological levels (31). Because the inhibition by L-lysine is competitive with respect to meso-diaminopimelate ( Fig.…”

Section: Discussionsupporting

confidence: 92%

“…3B), the concentration of diaminopimelate in the assay determines the amount of inhibitor required to reduce the activity of the enzyme. The sensitive assay method described here permitted the use of 0.1 mM diaminopimelate for assays, a concentration two orders of magnitude lower than that used in previous determinations of diaminopimelate decarboxylase (11,12,21,34,36) and more closely approximating physiological concentrations of the amino acid (13).…”

Section: Discussionmentioning

confidence: 96%

“…All previous investigations that cite the inhibition of diaminopimelate decarboxylase by L-lysine (11,12,21), except one (34), do not consider the possibility that this could have been an indirect consequence of competition for pyridoxal phosphate by primary amines (such as lysine). Indeed, Schiff base formations between pyridoxal phosphate and primary amines have been studied spectrophotometrically for some time (18,19).…”

Section: Discussionmentioning

confidence: 99%

“…1.20) has been shown to be repressed but not inhibited by L-lysine in the enteric bacteria (24,35). Subsequent studies have indicated that the enzyme from several species of nonenteric bacteria can be slightly inhibited by L-lysine (11,12,21,32), but only at relatively high concentrations (20 mM). This paper describes the characterization of diaminopimelate decarboxylase from the Marburg strain of Bacillus subtilis.…”

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confidence: 99%

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Control of lysine biosynthesis in Bacillus subtilis: inhibition of diaminopimelate decarboxylase by lysine

Rosner¹

1975

J Bacteriol

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Diaminopimelate decarboxylase has been characterized in extracts of Bacillus subtilis and resolved from aspartokinases I and II. Under certain conditions, the enzyme is specifically inhibited by physiological concentrations of L-lysine, but less specificity and altered kinetics of inhibition are observed if lower ionic strengths are employed in the assay procedure. Diaminopimelate decarboxylase can be desensitized to lysine inhibition by either lowering the pH or diluting the enzyme in Tris buffer in the absence of pyridoxal phosphate. Evidence is presented to indicate that, under proper conditions, lysine inhibition involves an interaction of the amino acid with the enzyme rather than competition for available pyridoxal phosphate in the assay. Lysine, by affecting the level of meso-diaminopimelate, may thus regulate its biosynthesis through sequential feedback inhibition. Analysis of the diaminopimelate decarboxylase of 15 revertants of mutants that had originally lacked diaminopimelate decarboxylase activity indicates that as little as 5% of the specific activity of enzyme observed in the wild-type strain is sufficient to permit normal growth rates. In the growing cell, diaminopimelate decarboxylase may therefore exist largely in an inhibited state.'4C]diaminopimelate (mixed isomers), amino acids, putrescine, and cadaverine were from Calbiochem; L-lysine methylester, N-ethylmaleimide, and ammonium sulfate were from Schwarz-Mann; p-hydroxymercuriphenylsulfonate was from Sigma; N-e-acetyl lysine was from Cyclo; 2-mercaptoethanol and phenethylamine were from Eastman; and pancreatic deoxyribonuclease (DNase) was from Worthington.Sephadex G-200 (40-120 $L) was treated by the method of Kawata and Chase (16) to remove fines. Enzyme assays. Diaminopimelate decarboxylase was assayed by the conversion of a, e-[1,7-'IC Idiaminopimelate to radioactive CO,. The following components were added to 25-ml Erlenmeyer flasks at 0 C, in a final volume of 2 ml: potassium phosphate, pH 8.3 (200 mM); triethanolamine hydrochloride, pH 8.3 (30 mM); potassium bicarbonate, pH 7.5 (10 mM); ethylenediaminetetraacetic acid (EDTA) (1 mM); pyridoxal phsophate (20 AM); ethylene glycol (15%); ['4C Idiaminopimelate (0.1 mM; 65,000 counts per min per smol of the mixed isomers); and appropriate amounts of enzyme. The flasks were then sealed with serum stoppers that supported plastic cups containing 0.2 ml of phenethylamine and a folded strip of glass fiber filter paper. After incubation at 25 C for 30 min, the flasks were cooled to 0 C and acidified by the injection of 1 ml of 2 N H,SO4. The flasks were allowed to equilibrate at 25 C for 30 min, whereupon the strips of filter paper 20 on July 15, 2020 by guest

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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Control of lysine biosynthesis in Bacillus subtilis: inhibition of diaminopimelate decarboxylase by lysine

Rosner¹

1975

J Bacteriol

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Fed-batch culture for L-lysine production via on-line state estimation and control

Liu

Tsao

1993

Bioprocess Engineering

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Into the metabolic wild: Unveiling hidden pathways of microbial metabolism

Ata,

Mattanovich

2024

Microbial Biotechnology

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Microbial metabolism has been deeply studied over decades and it is considered to be understood to a great extent. Annotated genome sequences of many microbial species have contributed a lot to generating biochemical knowledge on metabolism. However, researchers still discover novel pathways, unforeseen reactions or unexpected metabolites which contradict to the expected canon of biochemical reactions in living organisms. Here, we highlight a few examples of such non‐canonical pathways, how they were found, and what their importance in microbial biotechnology may be. The predictive power of metabolic modelling, well‐founded on biochemical knowledge and genomic information is discussed in the light of both discovery of yet unknown existing metabolic routes and the prediction of others, new to Nature.

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STUDIES ON LYSINE FERMENTATION III. Α, Ε-Diaminopimelic ACID ACCUMULATION AND DIAMINOPIMELIC ACID DECARBOXYLASE

Cited by 5 publications

References 5 publications

Control of lysine biosynthesis in Bacillus subtilis: inhibition of diaminopimelate decarboxylase by lysine

Control of lysine biosynthesis in Bacillus subtilis: inhibition of diaminopimelate decarboxylase by lysine

Fed-batch culture for L-lysine production via on-line state estimation and control

Into the metabolic wild: Unveiling hidden pathways of microbial metabolism

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