• BMB Reports
• /
• v.32 no.2
• /
• pp.210-213
• /
• 1999

In Serratia marcescens, acetolactate produced by the catabolic acetolactate synthase (ALS) is converted into acetoin, its physiological role of which is to maintain intracellular pH homeostasis. In this study, the expression mode of catabolic ALS by aeration and branched-chain amino acids was examined by the ELISA method. The amount of catabolic ALS decreased approximately 93% under aerobic conditions. We also showed that the expression of catabolic ALS decreased approximately 34 % and 65 % in the presence of 2.5 mM and 10 mM leucine, respectively. The repression of catabolic ALS by leucine has not been reported previously. In contrast to leucine, catabolic ALS levels increased approximately 13% and 38% by treatment with 2.5 mM and 10 mM isoleucine, respectively, while valine alone did not have any significant effect on the synthesis of catabolic ALS. The amount of catabolic ALS was also reduced to approximately 32% and 45% in the presence of 10 mM Leu+Ile and Leu+Ile+Val, respectively. The regulatory mode of the Serratia catabolic ALS suggests that catabolic ALS may also have a role in supplying acetolactate as an intermediate of valine and leucine biosynthesis in addition to the maintenance of internal pH.

• Journal of Nutrition and Health
• /
• v.25 no.3
• /
• pp.256-263
• /
• 1992

As various metabolic alterations develope in uremic patients. their diets need to be restricted, Furthermore medical complications with accompanying anorexia result in further complications and decrease in body strength. To assess the nutritional status of hemodialyzed patients we performed evaluation for dietary intake and protein catabolic rate(PCR) For 24 clinically stable male patients undergoing maintenance hemodialysis dietary intake was estimated by 3-day food record method and PCR was calculated with blood urea nitrogen at pre and post hemodialysis. The results were as follows : 1) Average daily energy and protein intake were 26.7$\pm$5.1kcal/kg of body weight. 0.95$\pm$0.19 g/kg of body weight respectively. 2) Protein catabolic rate calculated from interdialysis blood urea nitrogen levels was 1.00$\pm$0.20g/kg of body weight. Protein catabolic rate was correlated with the amount of Protein intake(r=0.44 p<0.05) 3) Relative body weight(RBW) of the subjects was smaller than that of healthy man without hemodialysis. Calorie and protein intake and protein catabolic rate were significantly different (p<0.05) between patients with lower RBW(<90% of ideal body weight) and those with normal RBW(90~110% of ideal body weight) and those with normal RBW(90~110% of iedal body weight) 4) The duration of hemodialysis did not have a significant effect on the nutritional status of the subjects.

• Journal of Microbiology and Biotechnology
• /
• v.32 no.12
• /
• pp.1527-1536
• /
• 2022

Escherichia coli can use allantoin as its sole nitrogen source under anaerobic conditions. The ureidoglycolate produced by double release of ammonia from allantoin can flow into either the glyoxylate shunt or further catabolic transcarbamoylation. Although the former pathway is well studied, the genes of the latter (catabolic) pathway are not known. In the catabolic pathway, ureidoglycolate is finally converted to carbamoyl phosphate (CP) and oxamate, and then CP is dephosphorylated to carbamate by a catabolic carbamate kinase (CK), whereby ATP is formed. We identified the ybcF gene in a gene cluster containing fdrA-ylbE-ylbF-ybcF that is located downstream of the allDCE-operon. Reverse transcription PCR of total mRNA confirmed that the genes fdrA, ylbE, ylbF, and ybcF are co-transcribed. Deletion of ybcF caused only a slight increase in metabolic flow into the glyoxylate pathway, probably because CP was used to de novo synthesize pyrimidine and arginine. The activity of the catabolic CK was analyzed using purified YbcF protein. The V_max is 1.82 U/mg YbcF for CP and 1.94 U/mg YbcF for ADP, and the K_M value is 0.47 mM for CP and 0.43 mM for ADP. With these results, it was experimentally revealed that the ybcF gene of E. coli encodes catabolic CK, which completes anaerobic allantoin degradation through substrate-level phosphorylation. Therefore, we suggest renaming the ybcF gene as allK.

• Journal of the Korean Society of Food Science and Nutrition
• /
• v.30 no.6
• /
• pp.127-127
• /
• 2001

• BMB Reports
• /
• v.31 no.2
• /
• pp.139-143
• /
• 1998

The catabolic ${\alpha}-acetolactate$ synthase purified from Serratia marcescens ATCC 25419 was rapidly inactivated by the tryptophane-specific reagent, N -bromosuccinimide, and the arginine-specific reagent, phenylglyoxal. The enzyme was inactivated slowly by the cysteine-specific reagent N-ethylmaleimide. The second-order rate constants for the inactivation by N-bromosuccinimide, phenylglyoxal. and N -ethylmaleimide were $114,749M^{-1}min^{-1}$, $304.3M^{-1}min^{-1}$, and $5.1M^{-1}min^{-1}$, respectively. The reaction order with respect to N-bromosuccinimide, phenylglyoxal, and N-ethylmaleimide were 1.5,0.71, and 0.86, respectively. The inactivation of the catabolic aacetolactate synthase by these modifying reagents was protected by pyruvate. These results suggest that essential tryptophane, arginine, and cysteine residues are located at or near the active site of the catabolic ${\alpha}-acetolactate$ synthase.

• The Korean Journal of Mycology
• /
• v.13 no.4
• /
• pp.235-241
• /
• 1985

The present study was designed to investigate biosynthetic patterns of polysaccharides under catabolic repression and derepression in Saccharomyces uvarum. Correlation coefficients between polysaccharide synthesis and polyphosphate accumulation were examined, according to the culture phase and under various phosphate concentrations (free, limited, sufficient). During catabolic derepression, biosynthesis of glycogen was enhanced. rapidly and highly in the cells grown on minimal medium, compared with those grown on the complete medium. Acid soluble glycogen type was the main component of total glycogen and alkali soluble glycogen was synthesized in small amount, after 24 hr culture, at the time of almost exhaustion of sugar in the medium. Total glycogen was accumulated highly in proportion to the amount of phosphate added to the medium. It could be postulated that type 'C' isoenzyme among ALPase was directly or indirectly correlated with the glucan synthesis. Mannan synthesis indicated maximal amount at the early exponential phase and stationary phase, and also acid soluble sugars at the stationary phase. Correlation coefficient between the mannan synthesis and poly-p-'C' accumulation, and also between mannan synthesis and phospholipid content indicated 0.866 and 0.726, respectively.

• BMB Reports
• /
• v.31 no.1
• /
• pp.37-43
• /
• 1998

The catabolic ${\alpha}$-acetolactate synthase was purified to homogeneity from Serratia marcescens ATCC 25419 using ammonium sulfate fractionation, DEAE-Sepharose, Phenyl-Sepharose, and Hydroxylapatite column chromatography. The native molecular weight of the enzyme was approximately 150 kDa and composed of two identical subunits with molecular weights of 64 kDa each. The N-terminal amino acid sequence of the enzyme was determined to be Ala-Gln-Glu-Lys-Thr-Gly-Asn-Asp-Trp-Gln-His-Gly-Ala-Asp-Leu-Val-Val-Lys-Asn-Leu. It was not inhibited by the branched chain amino acids and sulfometuron methyl herbicide. The optimum pH of the enzyme was around pH 5.5 and the pI value was 6.1. The catabolic ${\alpha}$-acetolactate synthase showed weak immunological relationships with recombinant tobacco ALS, barley ALS, and the valine-sensitive ALS isozyme from Serratia marcescens.

• Journal of Microbiology and Biotechnology
• /
• v.28 no.7
• /
• pp.1037-1051
• /
• 2018

The genus Rhodococcus is a phylogenetically and catabolically diverse group that has been isolated from diverse environments, including polar and alpine regions, for its versatile ability to degrade a wide variety of natural and synthetic organic compounds. Their metabolic capacity and diversity result from their diverse catabolic genes, which are believed to be obtained through frequent recombination events mediated by large catabolic plasmids. Many rhodococci have been used commercially for the biodegradation of environmental pollutants and for the biocatalytic production of high-value chemicals from low-value materials. Recent studies of their physiology, metabolism, and genome have broadened our knowledge regarding the diverse biotechnological applications that exploit their catabolic enzymes and pathways.

• Macromolecular Research
• /
• v.16 no.1
• /
• pp.1-5
• /
• 2008

The enzymatic hydrolysis of chitin has been studied for almost a century, and early work established that at least two enzymes are required, a chitinase that mainly yields the disaccharide N,N'-diacetylchitobiose, or $(GlcNAc)_2$, and a "chitobiase", or ${\beta}$-N-acetylglucosaminidase, which gives the final product G1cNAc. This pathway has not been completely identified but has remained the central concept for the chitin catabolism through the $20^{th}$ century1 including in marine bacteria. However, the chitin catabolic cascade is quite complex, as described in this review. This report describes three biologically functional genes involved in the chitin catabolic cascade of Vibrios in an attempt to better understand the metabolic pathway of chitin.

• Journal of Microbiology
• /
• v.43 no.6
• /
• pp.572-576
• /
• 2005

This study focused on detecting catabolic genes for polycyclic aromatic hydrocarbons (PAHs) distributed in the reed rhizosphere of Sunchon Bay, Korea. These marsh and mud environments were severely affected by human activities, including agriculture and fisheries. Our previous study on microbial roles in natural decontamination displayed the possibility that PAH-degrading bacteria, such as Achromobacter sp., Alcaligenes sp., Burkholderia sp. and Pseudomonas sp. play an important decontamination role in a reed rhizosphere. In order to gain further fundamental knowledge on the natural decontamination process, catabolic genes for PAH metabolism were investigated through PCR amplification of dioxygenase genes using soil genomic DNA and sequencing. Comparative analysis of predicted amino acid sequences from 50 randomly selected dioxygenase clones capable of hydroxylating inactivated aromatic nuclei indicated that these were divided into three groups, two of which might be originated from PAH-degrading bacteria. Amino acid sequences of each dioxygenase clone were a part of the genes encoding enzymes for initial catabolism of naphthalene, phenanthrene, or pyrene that might be originated from bacteria in the reed rhizosphere of Sunchon Bay.