• 제목/요약/키워드: pyridoxal 5'-phosphate (PLP)

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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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    • v.8 no.6
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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.

Inactivation of Brain myo-Inositol Monophosphate Phosphatase by Pyridoxal-5'-Phosphate

  • Kim, Dae-Won;Hong, Joung-Woo;Eum, Won-Sik;Choi, Hee-Soon;Choi, Soo-Hyun;Kim, So-Young;Lee, Byung-Ryong;An, Jae-Jin;Lee, Sun-Hwa;Lee, Seung-Ree;Kwon, Oh-Shin;Kwon, Hyeok-Yil;Cho, Sung-Woo;Lee, Kil-Soo;Park, Jin-Seu;Choi, Soo-Young
    • BMB Reports
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    • v.38 no.1
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    • pp.58-64
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    • 2005
  • Myo-inositol monophosphate phosphatase (IMPP) is a key enzyme in the phosphoinositide cell-signaling system. This study found that incubating the IMPP from a porcine brain with pyridoxal-5'-phosphate (PLP) resulted in a time-dependent enzymatic inactivation. Spectral evidence showed that the inactivation proceeds via the formation of a Schiff's base with the amino groups of the enzyme. After the sodium borohydride reduction of the inactivated enzyme, it was observed that 1.8 mol phosphopyridoxyl residues per mole of the enzyme dimer were incorporated. The substrate, myo-inositol-1-phosphate, protected the enzyme against inactivation by PLP. After tryptic digestion of the enzyme modified with PLP, a radioactive peptide absorbing at 210 nm was isolated by reverse-phase HPLC. Amino acid sequencing of the peptide identified a portion of the PLP-binding site as being the region containing the sequence L-Q-V-S-Q-Q-E-D-I-T-X, where X indicates that phenylthiohydantoin amino acid could not be assigned. However, the result of amino acid composition of the peptide indicated that the missing residue could be designated as a phosphopyridoxyl lysine. This suggests that the catalytic function of IMPP is modulated by the binding of PLP to a specific lysyl residue at or near its substrate-binding site of the protein.

뇌조직으로부터 정제한 Glutamate decarboxylase의 활성부위 구조 연구

  • 최수영;이수진;장상호;이길수;위세찬
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1994.04a
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    • pp.270-270
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    • 1994
  • 돼지 뇌조직으로부터 순수 분리 정제된 Glutamate decarboxylase (GAD)는 효소 dimer당 0.8mole 보조 인자인 pyridoxal-5-phosphate(PLP)가 강하게 binding되어 있었다. 이러한 부분적으로 resolved된 효소에 외부로부터 PLP를 넣어주면 효소의 활성도는 최대값으로 증가하였다. 정제된 GAD는 sulfydryl시약에 의한 화학변형에 의하여 효소의 활성도를 상실하였으며 환원제인 dithiothreitol이나 2-mercaptoethanol의 첨가에 의하여 효소의 활성도가 복구되는 것으로 보아 효소의 활성부위의 활성에 직접 관여하는 중요한 cysteinyl잔기가 존재하고 있는 것을 알 수 있다.

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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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    • v.5 no.1
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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.

Vitamin B6 Deficiency, Genome Instability and Cancer

  • Wu, Xia-Yu;Lu, Lin
    • Asian Pacific Journal of Cancer Prevention
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    • v.13 no.11
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    • pp.5333-5338
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    • 2012
  • Vitamin B6 functions as a coenzyme in >140 enzymatic reactions involved in the metabolism of amino acids, carbohydrates, neurotransmitters, and lipids. It comprises a group of three related 3-hydroxy-2-methyl-pyrimidine derivatives: pyridoxine (PN), pyridoxal (PL), pyridoxamine (PM) and their phosphorylated derivatives [pyridoxal 5'-phosphate (PLP) and pyridoxamine 5'-phosphate (PMP)], In the folate metabolism pathway, PLP is a cofactor for the mitochondrial and cytoplasmic isozymes of serine hydroxymethyltransferase (SHMT2 and SHMT1), the P-protein of the glycine cleavage system, cystathionine ${\beta}$-synthase (CBS) and ${\gamma}$-cystathionase, and betaine hydroxymethyltransferase (BHMT), all of which contribute to homocysteine metabolism either through folate-mediated one-carbon metabolism or the transsulfuration pathway. Folate cofactors carry and chemically activate single carbons for the synthesis of purines, thymidylate and methionine. So the evidence indicates that vitamin B6 plays an important role in maintenance of the genome, epigenetic stability and homocysteine metabolism. This article focuses on studies of strand breaks, micronuclei, or chromosomal aberrations regarding protective effects of vitamin B6, and probes whether it is folate-mediated one-carbon metabolism or the transsulfuration pathway for vitamin B6 which plays critical roles in prevention of cancer and cardiovascular disease.

Chemical Modification of the Biodegradative Threonine Dehydratase from Serratia marcescens with Arginine and Lysine Modification Reagents

  • Choi, Byung-Bum;Kim, Soung-Soo
    • BMB Reports
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    • v.28 no.2
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    • pp.124-128
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    • 1995
  • Biodegradative threonine dehydratase purified from Serratia marcescens ATCC 25419 was inactivated by the arginine specific modification reagent, phenylglyoxal (PGO) and the lysine modification reagent, pyridoxal 5'-phosphate (PLP). The inactivation by PGO was protected by L-threonine and L-serine. The second order rate constant for the inactivation of the enzyme by PGO was calculated to be 136 $M^{-1}min^{-1}$. The reaction order with respect to PGO was 0.83. The inactivation of the enzyme by PGO was reversed upon addition of excess hydroxylamine. The inactivation of the enzyme by PLP was protected by L-threonine, L-serine, and a-aminobutyrate. The second order rate constant for the inactivation of the enzyme by PLP was 157 $M^{-1}min^{-1}$ and the order of reaction with respect to PLP was 1.0. The inactivation of the enzyme by PLP was reversed upon addition of excess acetic anhydride. Other chemical modification reagents such as N-ethylmaleimide, 5,5'-dithiobis (2-nitrobenzoate), iodoacetamide, sodium azide, phenylmethyl sulfonylfluoride and diethylpyrocarbonate had no effect on the enzyme activity. These results suggest that essential arginine and lysine residues may be located at or near the active site.

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Reaction of Phospholipid with Brain Glutamate Decarboxylase

  • Lee, B.R.;Jang, S.H.;Song, M.S.;S.Wee;Park, E.Y.;Lee, K.S.;Park, S.Y.
    • Proceedings of the Korean Society of Applied Pharmacology
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    • 1995.04a
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    • pp.73-73
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    • 1995
  • We investigated the effect of derivatized phospholipid, P-pyridoxyl dipalmiuylphosphatidylethanolamine (P-pyr-DPPE), on the catalytic activity of purified porcine brain glutamate decarboxylase(GAD) which catalyzes the synthesis of GABA known as major inhibitory neurotransmitter in CNS. When the P-pyr-DPPE was incorporated into dipalmitdylphosphatidylcholine(DPPC) or phosphatidylserine(PS) vesicles, these vesicles enhanced the catalytic activity of GAD. P-pyr-DPPE also interacted with apoglutamate decarboxylase(apoGAD) and produced the free pyridoxal-5-phosphate(PLP) which is the natural cofactor of GAD. This result indicated that apoGAD catalyzed the cleavage reaction of the P-pyridoxyl moiety of the derivatized phopholipid to generate free PLP, and then free PLP bound to the apoGAD resulting in restroration of the catalytic activity of the enzyme.

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

  • 안홍석
    • Journal of Nutrition and Health
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    • v.33 no.3
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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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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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    • v.16 no.9
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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.

The Effect of Allium Vegetable Intake on the Redistribution of Pyridoxal 5'-phosphate Levels in Exercising Rats

  • Cho Youn-Ok;Yoon Mi-Kyung
    • Nutritional Sciences
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    • v.8 no.3
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    • pp.169-174
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    • 2005
  • This study investigated the effect of allium vegetable intake on the storage and utilization of energy substrates before, during, and after exercise in tissues of rats. Ninety mts were fed either a control diet or a diet with added allium sativum (AS), allium cepa (AC), allium fistulosum (AF), or allium tuberosum (AT) for 4 weeks and then subdivided into 3 groups: before-exercise (BE) during-exercise (DE) after-exercise (AE). The DE group exercised on treadmill for 1 hour just before being sacrificed at the end of the 4th week of the dietary treatment Rats in the AE group were allowed to recuperate for 2 horns after being exercised like the DE group. Pyriooxal 5'-phospwe (PLP) levels were compared in plasma, liver and skeletal muscle of rats. There was no difference between AS animals and control animals in plasma PLP levels regardless of exercise. The plasma PLP levels of AC animals were higher than those of control animals before exercise but this PLP was decreased with exercise and lower than that of control animals after exercise. The plasma PLP levels of AF animals were higher than those of control animals during exercise but there was no difference before and after exercise. The plasma PLP levels of AT animals were higher than those of control animals regardless of exercise. Compared to those of control mts, the PLP levels of liver and muscle were significantly lower in AS, AC, AF and AT mts before exercise. The levels of liver PLP were significantly decreased in control mts while not changed in AS, AC, AF and AT mts during exercise. The levels of liver PLP tended to decrease in AS, AC and AF mts after exercise. The levels of muscle PLP were significantly decreased in control rats, while not changed in AS, AC and AF mts during exercise. The levels of muscle PLP were decreased in control mts but not changed in AS, AC and AF mts after exercise. Thus, it is suggested that the changes of PLP concentrations in plasma and tissues induced by exercise are affected by allium vegetable diet and demonstrated that allium vegetable intake induced an alteration in the redistribution of PLP among tissues.