Hideyuki Suzuki

Hideyuki Suzuki
Kyoto Institute of Technology · Graduate School of Science and Technology

PhD

About

151
Publications
13,082
Reads
How we measure 'reads'
A 'read' is counted each time someone views a publication summary (such as the title, abstract, and list of authors), clicks on a figure, or views or downloads the full-text. Learn more
4,182
Citations
Citations since 2017
11 Research Items
1528 Citations
20172018201920202021202220230100200300
20172018201920202021202220230100200300
20172018201920202021202220230100200300
20172018201920202021202220230100200300
Additional affiliations
September 2007 - present
Kyoto Institute of Technology
Position
  • Professor (Full)

Publications

Publications (151)
Article
A plasmid was constructed to express the CapA-SpeA fusion protein from the capA gene, which encodes one of the subunits of capsular poly-γ-glutamate synthetase of Bacillus subtilis subsp. natto, and the speA gene, encoding biosynthetic arginine decarboxylase (EC 4.1.1.19) of Escherichia coli, under the control of the T5 promoter. The expression of...
Article
Full-text available
In the bio-based polymer industry, putrescine is in the spotlight for use as a material. We constructed strains of Escherichia coli to assess its putrescine production capabilities through the arginine decarboxylase pathway in batch fermentation. N -Acetylglutamate (ArgA) synthase is subjected to feedback inhibition by arginine. Therefore, the 19th...
Article
The enzymatic characteristics of γ-glutamyltranspeptidase were elucidated. The catalytic nucleophile of the enzymatic reaction of Escherichia coli γ-glutamyltranspeptidase was identified as the Oγ of the N-terminal Thr-residue of the small subunit. It was demonstrated that the inactive precursor of γ-glutamyltranspeptidase is processed autocatalyti...
Article
Polyamines are essential for biofilm formation in Escherichia coli , but it is still unclear which polyamines are primarily responsible for this phenomenon. To address this issue, we constructed a series of E. coli K-12 strains with mutations in genes required for the synthesis and metabolism of polyamines. Disruption of the spermidine synthase gen...
Article
Escherichia coli strain, whose gene is one of the subunits of succinate dehydrogenase (sdhA), and gene of the transcriptional repressor of isocitrate lyase (iclR) were disrupted, accumulated 6.6 times as much intracellular succinate as the wild-type MG1655 strain in aerobic growth, but succinate was not found in the culture medium. E. coli citT gen...
Article
γ-Glutamyltranspeptidase (GGT) has been widely used as a marker enzyme of hepatic and biliary diseases and relations between various diseases and its activity have been studied extensively. Nevertheless, several of its fundamental enzymatic characteristics had not been elucidated. We obtained homogeneous preparation of GGTs from bacteria, character...
Article
We found that shochu slop, the residue generated during production of distilled shochu liquor, which must be treated as industrial waste, can be used as an excellent medium for E. coli culture. LB medium is generally used in laboratories for culturing E. coli. However, it is not the optimal medium for E. coli culture because the bacterial cells can...
Article
In the present study, we demonstrate a novel use for a commercially available glutaminase that can be used as a γ-glutamyltranspeptidase in kokumi seasoning production. Soy protein and gluten were hydrolyzed using a protease isolated from Bacillus licheniformis. The resulting protein hydrolysates were γ-glutamylated with a γ-glutamyltranspeptidase,...
Article
Full-text available
Recent research has suggested that polyamines (putrescine, spermidine, and spermine) in the intestinal tract impact the health of animals either negatively or positively. The concentration of polyamines in the intestinal tract results from the balance of uptake and export of the intestinal bacteria. However, the mechanism of polyamine export from b...
Article
γ-Glutamyl transpeptidase (GGT, EC 2.3.2.2) that catalyzes the hydrolysis and transpeptidation of glutathione and its S-conjugates is involved in a number of physiological and pathological processes through glutathione metabolism and is an attractive pharmaceutical target. We report here the evaluation of a phosphonate-based irreversible inhibitor,...
Chapter
Polyamines play important roles in cell growth and proliferation. In particular, these biogenic compounds are involved in the regulation of transcription and translation processes required for bacterial proliferation. Consequently, intracellular polyamine content is strictly regulated at several levels, including biosynthesis, degradation, and upta...
Chapter
Many bacteria take up external polyamines to optimize their growth and adaptation to the environment. Furthermore, cell-to-cell communication using polyamines recently reported requires export of polyamines and uptake or recognition of polyamine outside the cell. At physiological pH, polyamines are positively charged and hydrophilic and therefore c...
Article
Full-text available
Members of polyamine modulon whose synthesis is enhanced at the level of translation were looked for under oxidative stress conditions caused by 0.6 μM K2TeO3. When an Escherichia coli polyamine-requiring mutant MA261 was cultured in the presence of K2TeO3, the degree of polyamine stimulation of cell growth was greater than in cells cultured in the...
Book
This book covers key topics in polyamine research from a range of organisms, including plants, mammals, and prokaryotes such as bacteria and archaea. The book provides an introduction to general concepts in the field of polyamine research, as well as more detailed information. With the availability of genome sequence data from a broad range of orga...
Article
γ-Glutamyltranspeptidase (GGT; EC 2.3.2.2) is involved in the degradation of γ-glutamyl compounds such as glutathione (GSH; γ-glutamyl-cysteinyl-glycine) . A major physiological role of this enzyme is to cleave the extracellular GSH as a source of cysteine for intracellular glutathione biosynthesis. Another crucial role of GGT is to cleave glutathi...
Article
Full-text available
Prevention of quality of life (QOL) deterioration is associated with the inhibition of geriatric diseases and the regulation of brain function. However, no substance is known that prevents the aging of both body and brain. It is known that polyamine concentrations in somatic tissues (including the brain) decrease with increasing age, and polyamine-...
Article
Full-text available
γ-Glutamyltranspeptidase (GGT) is an enzyme that plays a central role in glutathione metabolism, and acivicin is a classical inhibitor of GGT. Here, the structure of acivicin bound to Bacillus subtilis GGT determined by X-ray crystallography to 1.8 Å resolution is presented, in which it binds to the active site in a similar manner to that in Helico...
Article
Properties of putrescine uptake by PotFGHI and PuuP and their physiological significance were studied using a polyamine biosynthesis and uptake deficient Escherichia coli KK3131 transformed with pACYC184 containing potFGHI or puuP. Putrescine uptake activity of E. coli KK3131 transformed with pACYC184-PotFGHI was higher than that of E. coli 3131 tr...
Article
γ-Glutamyltranspeptidase (GGT) hydrolyzes γ-glutamyl compounds and transfers their γ-glutamyl moieties to amino acids and peptides. We previously showed that the “umami” taste of soy sauce could be improved by the addition of salt-tolerant Bacillus subtilis GGT to the fermentation mixture, “moromi”. Although miso fermentation is a semi-solid fermen...
Article
Full-text available
Previously, we reported that the speA gene, encoding arginine decarboxylase, is required for swarming in the urinary tract pathogen Proteus mirabilis. In addition, this previous study suggested that putrescine may act as a cell-to-cell signaling molecule (Sturgill, G., and Rather, P. N. (2004) Mol. Microbiol. 51, 437–446). In this new study, PlaP,...
Article
More than a century has passed since Kikunae Ikeda identified sodium l-glutamate as the umami component of 'kombu', a kind of seaweed. Since then, many novel physiological functions and new applications of amino acids have been revealed. The biosynthetic pathways of amino acids are tightly controlled by several regulation mechanisms that ensure spe...
Article
Heat-treated γ-glutamyltranspeptidase of Escherichia coli recovered enzymatic activity after incubation at 4 °C, while heat-treated γ-glutamyltranspeptidase of Bacillus subtilis did not. Fluorescent spectra, CD spectra, and native polyacrylamide gel electrophoresis analysis suggested that the dimer of E. coli γ-glutamyltranspeptidase was separated...
Article
γ-Glutamyl transpeptidase (GGT) catalyzing the cleavage of γ-glutamyl bond of glutathione and its S-conjugates is involved in a number of physiological and pathological processes through glutathione homeostasis. Defining its Cys-Gly binding site is extremely important not only in defining the physiological function of GGT, but also in designing spe...
Article
Full-text available
In Escherichia coli, putrescine is metabolized to succinate for use as a carbon and nitrogen source by the putrescine utilization pathway (Puu pathway). One gene in the puu gene cluster encodes a transcription factor, PuuR, which has a helix-turn-helix DNA-binding motif. DNA microarray analysis of an E. coli puuR mutant, in which three amino acid r...
Article
Full-text available
Bifidobacteria inhabit the lower intestine of mammals including humans where the mucin gel layer forms a space for commensal bacteria. We previously identified that infant-associated bifidobacteria possess an extracellular membrane-bound endo-α-N-acetylgalactosaminidase (EngBF) that may be involved in degradation and assimilation of mucin-type olig...
Article
Full-text available
Recently, many studies have reported that polyamines play a role in bacterial cell-to-cell signaling processes. The present study describes a novel putrescine importer required for induction of type 1 pili-driven surface motility. The surface motility of the Escherichia coli ΔspeAB ΔspeC ΔpotABCD strain, which cannot produce putrescine and cannot i...
Article
Full-text available
Bacillus S11 (BS11), a Gram-positive spore forming bacteria, was identified as Bacillus subtilis, based on biochemical tests, physical morphology, and 16S rRNA gene sequence. BS11 was found to be safe as probiotic for shrimp because it does not produce either detectable antimicrobial substance or enterotoxin. A potential specific markers of BS11 by...
Article
The optimal reaction conditions for the synthesis of γ-glutamylglutamine using γ-glutamyltranspeptidase from Escherichia coli were determined. The maximum yield of γ-glutamylglutamine (110 mM) was obtained using 250 mM L: -glutamine and 1.1 U γ-glutamyltranspeptidase/ml at pH 10.5 and at 37°C for 7 h; the conversion of glutamine to γ-glutamylglutam...
Article
Full-text available
γ-Aminobutyrate (GABA) is metabolized to succinic semialdehyde by GABA aminotransferase (GABA-AT), and the succinic semialdehyde is subsequently oxidized to succinate by succinic semialdehyde dehydrogenase (SSADH). In Escherichia coli, there are duplicate GABA-ATs (GabT and PuuE) and duplicate SSADHs (GabD and YneI). While GabT and GabD have been w...
Article
Semisynthetic cephalosporins, the best-selling antibiotics worldwide, are derived from 7-aminocephalosporanic acid (7-ACA). Currently, in the pharmaceutical industrie, 7-ACA is mainly produced from cephalosporin C by sequential application of D-amino acid oxidase and cephalosporin acylase. Here we study the potential of industrially amenable enzyme...
Article
γ-Glutamyltranspeptidase (GGT; EC 2.3.2.2), an enzyme found in organisms from bacteria to mammals and plants, plays a central role in glutathione metabolism. Structural studies of GGTs from Escherichia coli and Helicobacter pylori have revealed detailed molecular mechanisms of catalysis and maturation. In these two GGTs, highly conserved residues f...
Article
In the last few decades, enzymatic production of 3,4-dihydroxyphenyl-L-alanine (L-dopa) using tyrosine phenol-lyase (Tpl) has been industrialized. This method has an intrinsic problem of tyrosine contamination because Tpl is synthesized under tyrosine-induced conditions. Herein, we constructed a hyper-L-dopa-producing strain by exploiting a mutant...
Article
In a previous work, it was observed that the swarming of polyamine-deficient Proteus mirabilis (speB::sm) was severely inhibited on Luria-Bertani (LB) swarming plates (LBSw) (LB, 0.5% glucose, 0.5% agar), and it was clarified that extracellular putrescine was important as a signaling molecule for the induction of swarming in P. mirabilis. However,...
Article
Full-text available
The Puu pathway is a putrescine utilization pathway involving gamma-glutamyl intermediates. The genes encoding the enzymes of the Puu pathway form a gene cluster, the puu gene cluster, and puuP is one of the genes in this cluster. In Escherichia coli, three putrescine importers, PotFGHI, PotABCD, and PotE, were discovered in the 1990s and have been...
Article
Full-text available
The transcriptional regulator TyrR is known to undergo a dimer-to-hexamer conformational change in response to aromatic amino acids, through which it controls gene expression. In this study, we identified N316D as the second-site suppressor of Escherichia coli TyrR(E274Q), a mutant protein deficient in hexamer formation. N316 variants exhibited alt...
Article
gamma-Glutamyltranspeptidase (GGT) catalyzes the cleavage of such gamma-glutamyl compounds as glutathione, and the transfer of their gamma-glutamyl group to water or to other amino acids and peptides. GGT is involved in a number of biological phenomena such as drug resistance and metastasis of cancer cells by detoxification of xenobiotics. Azaserin...
Article
Full-text available
Glutamate-putrescine ligase (γ-glutamylputrescine synthetase, PuuA, EC 6.3.1.11) catalyzes the γ-glutamylation of putrescine, the first step in a novel putrescine utilization pathway involving γ-glutamylated intermediates, the Puu pathway, in Escherichia coli. In this report, the character and physiological importance of PuuA are described. Purifie...
Article
Full-text available
7-Aminocephalosporanic acid (7-ACA) is an important material in the production of semisynthetic cephalosporins, which are the best-selling antibiotics worldwide. 7-ACA is produced from cephalosporin C via glutaryl-7-ACA (GL-7-ACA) by a bioconversion process using d-amino acid oxidase and cephalosporin acylase (or GL-7-ACA acylase). Previous studies...
Article
γ-Glutamyl-l-histidine was synthesized from l-glutamine and l-histidine by γ-glutamyltranspeptidase (EC 2.3.2.2) from Escherichia coli K-12. The optimum conditions for the production of γ-glutamyl-l-histidine are determined. The yield of γ-glutamyl-l-histidine synthesized under the optimum conditions was 48% with both substrates (41.2 g/l). The pro...
Article
γ-Glutamyltranspeptidase (GGT) catalyzes the hydrolysis of γ-glutamyl compounds and transfer of their γ-glutamyl moieties to amino acids and peptides. GGT is able to catalyze the hydrolysis of glutamine (Gln) to glutamic acid (Glu), the so called glutaminase reaction. A salt-tolerant wild-type GGT from Bacillus subtilis and D445A mutant GGT, whose...
Article
Full-text available
Gamma-glutamyltranspeptidase (GGT) is an extracellular enzyme that plays a key role in glutathione metabolism. The mature GGT is a heterodimer consisting of L- and S-subunits that is generated by posttranslational cleavage of the peptide bond between Gln-390 and Thr-391 in the precursor protein. Thr-391, which becomes the N-terminal residue of the...
Article
Some amino acids and peptides, which have low solubility in water, become much more soluble following gamma-glutamylation. Compounds become more stable in the blood stream with gamma-glutamylation. Several gamma-glutamyl compounds are known to have favorable physiological effects on mammals. Gamma-glutamylation can improve taste and can stabilize g...
Article
γ-Glutamyltranspeptidase (GGT) is an extracellular enzyme that plays a key role in glutathione metabolism. The mature GGT is a heterodimer consisting of L- and S-subunits that is generated by posttranslational cleavage of the peptide bond between Gln-390 and Thr-391 in the precursor protein. Thr-391, which becomes the N-terminal residue of the S-su...
Article
Full-text available
Helicobacter pylorigamma-glutamyltranspeptidase (HpGT) is a glutathione-degrading enzyme that has been shown to be a virulence factor in infection. It is expressed as a 60-kDa inactive precursor that must undergo autocatalytic processing to generate a 40-kDa/20-kDa heterodimer with full gamma-glutamyl amide bond hydrolase activity. The new N termin...
Article
Gamma-glutamyl transpeptidase (GGT, EC 2.3.2.2) catalyzes the hydrolysis and transpeptidation of extracellular glutathione and plays a central role in glutathione homeostasis. We report here the synthesis and evaluation of a series of hydrolytically stable gamma-(monophenyl)phosphono glutamate analogues with varying electron-withdrawing para substi...
Article
Full-text available
γ-Glutamyltranspeptidase (GGT) is a heterodimic enzyme that is generated from the precursor protein through posttranslational processing and catalyzes the hydrolysis of γ-glutamyl bonds in γ-glutamyl compounds such as glutathione and/or the transfer of the γ-glutamyl group to other amino acids and peptides. We have determined the crystal structure...
Article
gamma-Glutamyl-gamma-aminobutyrate hydrolase (PuuD) was purified and the properties of the enzyme were characterized. The active center of PuuD was identified as Cys-114 by site-directed mutagenesis. The expression of PuuD was induced by putrescine and O2 (substrates of the Puu pathway), while the addition of succinate or NH4Cl (products of the Puu...
Article
An effective protein expression system was constructed in Escherichia coli using the promoter of the tyrosine phenol-lyase (tpl) gene of Erwinia herbicola. This system involves a mutant form of the TyrR protein with an enhanced ability to activate tpl and the TutB protein with an ability to transport L-tyrosine (an inducer of Tpl). The highest expr...
Article
Full-text available
Glutathione protects cells and organisms from oxygen species and peroxides and is indispensable for aerobically living organisms. Moreover, it acts against xenobiotics and drugs by the formation and excretion of glutathione S conjugates. In this study, we show that the yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a glutathione transpo...
Article
The enzymatic production of 3,4-dihydroxyphenyl-L-alanine (L-DOPA) using Erwinia herbicola cells involves the action of tyrosine phenol-lyase (Tpl, EC 4.1.99.2). Since Tpl is only synthesized under L-tyrosine-induced conditions, the addition of L-tyrosine to the medium is unavoidable when preparing cells (the enzyme source), but severely impedes th...
Article
Full-text available
A novel bacterial putrescine utilization pathway was discovered. Seven genes, the functions of whose products were not known, are involved in this novel pathway. Five of them encode enzymes that catabolize putrescine; one encodes a putrescine importer, and the other encodes a transcriptional regulator. This novel pathway involves six sequential ste...
Article
Full-text available
The aspartyl residue at position 433 of γ-glutamyltranspeptidase of Escherichia coli K-12 was replaced by an asparaginyl residue. This substitution enabled γ-glutamyltranspeptidase to deacylate glutaryl-7-aminocephalosporanic acid, producing 7-aminocephalosporanic acid, which is a starting material for the synthesis of semisynthetic cephalosporins.
Article
The growth of Escherichia coli is inhibited by an antibiotic compound, azaserine (O-diazoacetyl-L-serine). Previous studies revealed the biochemical properties of azaserine, which involves inhibition of various enzymatic reactions as well as introduction of DNA breakage. However, genetically, nothing has been elucidated except that all the azaserin...
Article
Gamma-D-Glutamyl-L-tryptophan (SCV-07) is a prospective medicine for the treatment of tuberculosis, according to the phase two clinical trial. Because gamma-D-glutamyl-L-tryptophan has several reactive groups in its molecule, consists of D- and L-amino acids, and is connected by gamma-glutamyl linkage, its chemical synthesis is complicated. An effi...
Article
The taste of several bitter amino acids is reduced, sourness produced, and preference increased by gamma-glutamylization. An enzymatic method for synthesizing gamma-Glu-Val involving bacterial gamma-glutamyltranspeptidase (GGT) was developed. The optimum reaction conditions for the synthesis of gamma-Glu-Val were 20 mM Gln, 300 mM Val, and 0.04 U/m...
Article
Full-text available
γ-Glutamyltranspeptidase (EC 2.3.2.2) of Bacillus subtilis, which is an extracellular enzyme, hydrolyzes the γ-glutamyl linkage of glutathione. YwrD, which is homologous to γ-glutamyltranspeptidase, was speculated to have a similar physiological role. It was shown that γ-glutamyltranspeptidase, but not YwrD, is important in utilizing glutathione as...
Article
Full-text available
In Escherichia coli, the active transport of phenylalanine is considered to be performed by two different systems, AroP and PheP. However, a low level of accumulation of phenylalanine was observed in an aromatic amino acid transporter-deficient E. coli strain (ΔaroP ΔpheP Δmtr Δtna ΔtyrP). The uptake of phenylalanine by this strain was significantl...
Article
Full-text available
An enzymatic method for synthesizing various γ-d-glutamyl compounds efficiently and stereospecifically involving bacterial γ-glutamyltranspeptidase (EC 2.3.2.2) with d-glutamine as a γ-glutamyl donor was developed. With d-glutamine as a γ-glutamyl donor instead of l-glutamine in γ-glutamyltaurine synthesis, by-products such as γ-glutamylglutamine a...
Chapter
Bacterial gamma-glutamyltranspeptidase (GGT, EC 2.3.2.2) was applied to improve the taste of food. We found that the bitterness of amino acids was reduced, sourness produced, and preference increased with gamma-glutamylization. An enzymatic method for the synthesis of gamma-glutamyl amino acids involving GGT was developed. An enzymatic method invol...
Article
γ-Glutamyltranspeptidase (GGT) catalyzes the hydrolysis of γ-glutamyl compounds and the transfer of their γ-glutamyl moieties to amino acids and peptides. The transpeptidation activity of Bacillus subtilis GGT is about 10-fold higher than its hydrolysis activity. In B. subtilis GGT, substitution of Asp-445 with Ala abolished its transpeptidation ac...
Article
γ-Glutamyltranspeptidase (GGT) from Bacillus subtilis is an extracellular enzyme that exhibits glutaminase activity and is thus suitable for the fermentation of foods. As GGT of B. subtilis is synthesized only during the mid-stationary phase, which is inconvenient for industrial use, a strain overexpressing GGT for a sufficiently long period was ge...