• 제목/요약/키워드: pyridoxal

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Evaluation of vitamin $B_6$ intake and status of 20- to 64-year-old Koreans

  • Kim, Young-Nam;Cho, Youn-Ok
    • Nutrition Research and Practice
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    • 제8권6호
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    • pp.688-694
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    • 2014
  • BACKGROUND/OBJECTIVES: Recent research regarding vitamin $B_6$ status including biochemical index is limited. Thus, this study estimated intakes and major food sources of vitamin $B_6$; determined plasma pyridoxal 5'-phosphate (PLP); and assessed vitamin $B_6$ status of Korean adults. MATERIALS/METHODS: Three consecutive 24-h diet recalls and fasting blood samples were collected from healthy 20- to 64-year-old adults (n = 254) living in the Seoul metropolitan area, cities of Kwangju and Gumi, Korea. Vitamin $B_6$ intake and plasma PLP were analyzed by gender and by vitamin $B_6$ supplementation. Pearson's correlation coefficient was used to determine associations of vitamin $B_6$ intake and plasma PLP. RESULTS: The mean dietary and total (dietary plus supplemental) vitamin $B_6$ intake was $1.94{\pm}0.64$ and $2.41{\pm}1.45mg/day$, respectively. Median (50th percentile) dietary intake of men and women was 2.062 and 1.706 mg/day. Foods from plant sources provided 70.61% of dietary vitamin $B_6$ intake. Only 6.3% of subjects consumed total vitamin $B_6$ less than Estimated Average Requirements. Plasma PLP concentration of all subjects was $40.03{\pm}23.71nmol/L$. The concentration of users of vitamin $B_6$ supplements was significantly higher than that of nonusers (P < 0.001). Approximately 16% of Korean adults had PLP levels < 20 nmol/L, indicating a biochemical deficiency of vitamin $B_6$, while 19.7% had marginal vitamin $B_6$ status. Plasma PLP concentration showed positive correlation with total vitamin $B_6$ intake (r = 0.40984, P < 0.0001). CONCLUSIONS: In this study, vitamin $B_6$ intake of Korean adults was generally adequate. However, one-third of subjects had vitamin $B_6$ deficiency or marginal status. Therefore, in some adults in Korea, consumption of vitamin $B_6$-rich food sources should be encouraged.

Aspergillus oryzae에 있어서 L-Tyrosine의 분해효소에 관한 연구 (Studies on the Degradation of L-Tyrosine by Aspergillus oryzae)

  • 정동효;박성오;김영진
    • Applied Biological Chemistry
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    • 제14권2호
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    • pp.131-135
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    • 1971
  • 1. Aspergillus oryzae의 균체에는 L-tyrosine-${\alpha}$-ketoglutaric acid transaminase와 p-hydroxyphenlypyruvic acid oxidase가 존재해 있다. 2. L-Tyrosine 산화효소는 액침배양한 Aspergillus oryzae의 acetone powder, cell free extract 및 배양액에도 존재하며 L-tyrosine은 ${\alpha}$-ketoglutaric acid의 첨가로 더욱 빨리 전환되었다. 3. ${\alpha}$-Ketoglutaric acid와 pyridoxal phosphate는 transamination의 amino기의 수용체로 생각되었다. 4. 이들 효소계는 L-tyrosine와 p-hydroxyphenlypyruvic acid를 homogentisic acid로 산화시켰다. 5. Ascorbic acid는 p-hydroxyphenlypyruvic가 homogentisic acid로 산화되는데 특별한 역할을 하는 것 같다. 6. L-Tyrosine-${\alpha}$-ketoglutaric acid transaminase와 p-hydroxyphenlypyruvic acid oxidase의 최적 pH는 각 각 pH $6.0{\sim}6.5$와 pH 7.5이었다.

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임신 말 모체 및 제대혈의 비타민 $B_6$ 농도와 임신결과와의 상관성 (Relationships between Vitamin $B_6$ Status of Maternal-Umbilical Cord)

  • 안홍석
    • Journal of Nutrition and Health
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    • 제33권3호
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    • pp.263-270
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    • 2000
  • The purpose of this study was to evaluate the concentration of vitamin B6 in 16 pregnant-infant pairs and 15 nonpregnant women and to investigate the relationships between vitamin B6 status of maternal-umbilical cord plasma and pregnancy outcomes. dietary intake was obtained from semiquantitative frequency questionnaire. The daily mean energy and protein intakes were higher than the recommended dietary allowance, while daily vitamin B6 was only 74% of RDA in pregnant and 73% of RDA in nonpregnant women. The main sources of vitamin B6 were vegetables and fruits in pregnant women, while cereal and starch in nonpregnant women. The plasma PLP and PL levels of pregnant women were 14.85nmol/l and 20.56nmol/l, significantly lower than those of nonpregnant women. the PLP/PL ratios of pregnant and nonpregnant women were 1.65 and 0.33, indicating that the levels of vitamin B6 was altered during pregnancy. The PLP and PL levels of umbilical cord plasma were 63.55nmol/l and 32.25nmol/l, respectively. The vitamin B6 levels of umbilical cord plasma were significantly higher than that of maternal plasm. This finding indicates that the uptake of vitamin B6 in the fetus may be due to an active placental transport mechanism. The PLP level of maternal plasma correlated positively with that of umbilical cord plasma, showing the PLP concentration of umbilical cord plasma is affected by maternal vitamin B6 status. The maternal plasma PL level showed a positive correlation to infant birth weight. The positive association has bee also found between plasma PL level of umbilical cord and Apgar 1 min score.

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Assessment of vitamin $B_6$ status in Korean patients with newly diagnosed type 2 diabetes

  • Ahn, Hee-Jung;Min, Kyung-Wan;Cho, Youn-Ok
    • Nutrition Research and Practice
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    • 제5권1호
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    • pp.34-39
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    • 2011
  • The purpose of this study was to assess vitamin $B_6$ intake and status in Korean patients with newly diagnosed type 2 diabetes. Sixty-four patients with newly diagnosed type 2 diabetes and 8-11% glycated hemoglobin (A1C), along with 28 age-matched non-diabetic subjects, participated. Dietary vitamin $B_6$ intake was estimated by the 24 hour recall method and plasma pyridoxal 5'-phosphate (PLP) was measured. There was a significant difference in daily total calorie intake between the diabetic and non-diabetic groups ($1,917{\pm}376$ vs $2,093{\pm}311\;kcal$). There were no differences in intake of total vitamin $B_6$ ($2.51{\pm}0.91$ vs $2.53{\pm}0.81\;mg/d$) or vitamin $B_6$/1,000 kcal ($1.31{\pm}0.42$ vs $1.20{\pm}0.32\;mg$) between the diabetic and non-diabetic groups, and I intakes of total vitamin $B_6$ were above the Korean RDA in both groups ($180.0{\pm}57.9$ vs $179.0{\pm}65.4$). There was a higher percentage of diabetic subjects whose plasma PLP concentration was < 30 nmol/L compared to non-diabetic group. Plasma PLP levels tended to be lower in the diabetic subjects than in the non-diabetic subjects, although the difference was not statistically significant due to a large standard deviation ($80.0{\pm}61.2\;nmol/L$ vs $68.2{\pm}38.5\;nmol/L$). Nevertheless, plasma PLP levels should be monitored in pre-diabetic patients with diabetic risk factors as well as in newly diagnosed diabetic patients for long-term management of diabetes, even though this factor is not a major risk factor that contributes to the development of degenerative complications in certain patients.

Stabilization of Quinonoid Intermediate E-Q by Glu32 of D-Amino Acid Transaminase

  • Ro Hyeon-Su;Jeon Che-Ok;Kim Hak-Sung;Sung Moon-Hee
    • Journal of Microbiology and Biotechnology
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    • 제16권9호
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    • pp.1434-1440
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    • 2006
  • The stable anchorage of pyridoxal 5'-phosphate (PLP) in the active site of D-amino acid transaminase (D-AT) is crucial for the enzyme catalysis. The three-dimensional structure of D-AT revealed that Glu32 is one of the active site groups that may playa role in PLP binding. To prove the role of Glu32 in PLP stability, we firstly checked the rate of the potential rate-limiting step. The kinetic analysis showed that the rate of the ${\alpha}$-deprotonation step reduced to 26-folds in E32A mutant enzyme. Spectral analyses of the reaction of D-AT with D-serine revealed that the E32A mutant enzyme failed to stabilize the key enzyme-substrate intermediate, namely a quinonoid intermediate (E-Q). Finally, analysis of circular dichroism (CD) on the wild-type and E32A mutant enzymes showed that the optical activity of PLP in the enzyme active site was lost by the removal of the carboxylic group, proving that Glu32 is indeed involved in the cofactor anchorage. The results suggested that the electrostatic interaction network through the groups from PLP, Glu32, His47, and Arg50, which was observed from the three-dimensional structure of the enzyme, plays a crucial role in the stable anchorage of the cofactor to give necessary torsion to the plane of the cofactor-substrate complex.

Inhibitory actions of the antidepressant/antipanic drug phenelzine on brain GABA transaminase

  • Yoo, Byung-Kwon;Hong, Joung-Woo;Suk, Jae-Wook;Ahn, Jee-Yin;Yoo, Jeong-Suk;Lee, Kil-Soo;Cho, Sung-Woo;Choi, Soo-Young
    • Archives of Pharmacal Research
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    • 제19권6호
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    • pp.480-485
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    • 1996
  • Brain GABA transaminase is inactivated by preincubation with antidepressant/antipanic drug pheneizine (${\beta}$ethylphenylhydrazine) (mixing molar ratio 10:1) at pH 7.4. The reaction of enzyme with phenelzine was monitored by absorption and fluorescence spectroscopic methods. The inactive enzyme was fully reconstituted by addition of cofactor pyridoxal-5-phosphate. This result implies that the blocking of 1 mol of pyridoxal-5-phosphate per enzyme dimer is needed for inactivation of the enzyme. The time course of the reaction is significantly affected by the substrate .alpha.-ketoglutarate, which afforded complete protection against the loss of catalytic activity. The kinetic studies shows that phenelzine reacts with the cofactor of enzyme with a second-order rate constant of $2.1{\times}10^3M^{-1}s^{-1}$. It is postulated that the antidepressant/antipanic drug phenelzine is able to elevate the neurotransmitter GABA levels in central nervous system by inhibitory action on GABA degradative enzyme GABA transaminase.

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Characterization of a Potential Probiotic Lactiplantibacillus plantarum LRCC5310 by Comparative Genomic Analysis and its Vitamin B6 Production Ability

  • Yunjeong Lee;Nattira Jaikwang;Seong keun Kim;Jiseon Jeong;Ampaitip Sukhoom;Jong-Hwa Kim;Wonyong Kim
    • Journal of Microbiology and Biotechnology
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    • 제33권5호
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    • pp.644-655
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    • 2023
  • Safety assessment and functional analysis of probiotic candidates are important for their industrial applications. Lactiplantibacillus plantarum is one of the most widely recognized probiotic strains. In this study we aimed to determine the functional genes of L. plantarum LRCC5310, isolated from kimchi, using next-generation, whole-genome sequencing analysis. Genes were annotated using the Rapid Annotations using Subsystems Technology (RAST) server and the National Center for Biotechnology Information (NCBI) pipelines to establish the strain's probiotic potential. Phylogenetic analysis of L. plantarum LRCC5310 and related strains showed that LRCC5310 belonged to L. plantarum. However, comparative analysis revealed genetic differences between L. plantarum strains. Carbon metabolic pathway analysis based on the Kyoto Encyclopedia of Genes and Genomes database showed that L. plantarum LRCC5310 is a homofermentative bacterium. Furthermore, gene annotation results indicated that the L. plantarum LRCC5310 genome encodes an almost complete vitamin B6 biosynthetic pathway. Among five L. plantarum strains, including L. plantarum ATCC 14917T , L. plantarum LRCC5310 detected the highest concentration of pyridoxal 5'-phosphate with 88.08 ± 0.67 nM in MRS broth. These results indicated that L. plantarum LRCC5310 could be used as a functional probiotic for vitamin B6 supplementation.

Characterization of 1,4-Benzoquinone Reductase from Bovine Liver

  • Kim, Kyungsoon
    • Biotechnology and Bioprocess Engineering:BBE
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    • 제7권4호
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    • pp.216-220
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    • 2002
  • 1,4-Benzoquinone reductase was purified to electrophoretic homogeneity from bovine liver, and the purified enzyme found to have a molecular mass of 29 kDa, as determined by sodium dodecyl sulfate- polyacrylamide gel electrophoresis The enzyme exhibited pH optimum between 8.0 and 8.5. The apparent fm for 1,4-benzoqulnone was 1.643 mM, and the apparent Km for NADH was 1.837 mM. Various divalent cations, such as Hg$\^$2+/, Cu$\^$2+/, and Zn$\^$2+/, exhibited strong inhibitory effects. The enzyme activity was also strongly inhibited by quercetin, dicumarol, and benzoic acid. Incubation of the enzyme with N-bromosuccinimide and pyridoxal 5’-phosphate led to inhibitions of 100% and 99%, respectively. Accordingly, these results suggest that trypto-phan and Iysine residues are Involved at or near the active sites of the enzyme.

$\gamma$-Aminobutyrate Transaminase에 대한 Mycotoxin의 저해작용 (Inhibitory Actions of Mycotoxins on Brain $\gamma$-Aminobutyrate Transaminase)

  • Lee, Su-Jin;Lee, Kil-Soo;Choi, Soo-Young
    • 미생물학회지
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    • 제31권3호
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    • pp.224-229
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    • 1993
  • GABA transminase (4-aminobutyrate aminotransferase), which catalyzes the breakdown of the major inhibitory neurotransmitter, GABA, in mammalian brain, was inactivated by preincubation with the mycotoxin patulin. The time course of the reaction was significantly affected by the substrate .alpha.-ketoglutarate, which aforded complete protection against the loss of catalytic activity. The recovery from the inhibition of patulin by the addition of dithiothreitol (DTT) supports that patulin reacts with the sulfhydryl residue in the catalytic domain of the enzyme. The reconstitution of the reduced enzyme and apoenzyme with pyridoxal-5-P(PLP) was inhibited by another mycotoxin, penicilic acid. This mycotoxin may interact with lysyl residue of the enzyme. Therefore, it is postulated that the critical sulfhydryl and lysyl residues in the catalytic domain of the enzyme react with mycotoxin patulin and penicillic acid, respectively.

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Purification and Charactedrization of Cysteine Desulfhydrase from Streptomyces albidoflavus SMF301

  • Ryu, Jae-Gon;Kang, Sung-Gyun;Kim, In-Seop;Rho, Young-Taik;Lee, Sang-Hee;Lee, Kye-Joon
    • Journal of Microbiology
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    • 제35권2호
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    • pp.97-102
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    • 1997
  • Cysteine desulfhydrase (EC 4.4.1.1.) was purified from the culture supernatant of Streptomyces albidoflavus SMF301 by hydroxyapatite, gel filtration and Resource Q ion-exchange chromatography with a purification fold of six identical subunits. The enzyme was stabilized by dithiothreitol and pyridoxal 5'-phosphate during the purification procedures. The optimum pH and temperature were pH 8.6 and 35$^{\circ}C$, respectively. The N-terminal amino acid sequence was identified as A-P-L-P-T-A-D-V-R-S-D-P-G-Y-R-E-W-L-G-E-A-V. The purified cystein desulfhydrase had a high substrate specificity toward cysteine, and exhibited no cystahionine $\gamma$-lyase activity. The $K_m$ value for cysteine was determined to be 0.37 mM.

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