Đặt vấn đề: Bệnh thiếu men Glucose - 6 - Phosphate Dehydrogenase (G6PD) có tỷ lệ cao hơn ở những dân tộc sống trong vùng sốt rét lưu hành. Ninh Thuận là tỉnh có nhiều dân tộc sinh sống và có 61,8% dân số sống trong vùng dịch tễ sốt rét. Tuy nhiên, chưa có nghiên cứu về tình hình thiếu men G6PD. Chúng tôi tiến hành khảo sát tỷ lệ và đặc điểm dịch tễ học thiếu men G6PD ở sơ sinh để góp phần đề xuất biện pháp dự phòng biến chứng nguy hiểm của bệnh này. Mục...
Two enzymes control the rearrangement of carbon skeletons which result in the production of Glyceraldehyde-3-phosphate and Fructose-6-phosphate.
Transketolase transfers C2 units: TPP requiring enzyme like pyruvate dehydrogenase
Transaldolase transfers C3 units: uses a shiffs base with an active lysine group
The book takes in consideration some dehydrogenases, enzymes with different functions in the cells by using different substrates, such as hydroxysteroid dehydrogenases, aldehyde dehydrogenases, glucose-6-phosphate dehydrogenase, pyruvate dehydrogenase complex, glutamate dehydrogenase, succinate dehydrogenase. They are examined from the following points of view: biochemistry, physiological functions and role in some diseases and in the development of tumours. For these reasons, the book is divided into three sections: 1. Dehydrogenases and cancer 2. Dehydrogenases and some diseases 3.
The bifunctional enzyme glucose-6-phosphate dehydrogenase-6-phospho-gluconolactonase (G6PD-6PGL) found in Plasmodium falciparum has
unique structural and functional characteristics restricted to this genus.
This study was designed to examine the effects of RNA-mediated PfG6PD-6PGL gene silencing in cultures ofP. falciparumon the expression of para-site antioxidant defense genes at the transcription level.
The ÔMediterraneanÕ variant of glucose-6-phosphate dehydrogenase (G6PD) deﬁciency is due to the C563CT point mutation, leading to replacement of Ser with Phe at position 188, resulting in acute haemolysis triggered by oxidants. Previous work has shown increased formation of altered aspartate residues in membrane proteins during cell ageing and in response to oxidative stress in normal erythrocytes. These abnormal residues are speciﬁcally recognized by the repair enzyme L-isoaspartate (D-aspartate) protein O-methyltransferase (PCMT; EC 184.108.40.206). ...
Cloning and over-expression of human glucose 6-phosphate dehydrogenase (Glc6P dehydrogenase) has for the ﬁrst time allowed a detailed kinetic study of a preparation that is genetically homogeneous and in which all the protein molecules are of identical age. The steady-state kinetics of the recombinant enzyme, studied by ﬂuorimetric initial-rate measurements, gave converging linear Lineweaver–Burk plots as expected for a ternary-complex mechanism.
Possible binding proteins of CP12 in a green alga,Chlamydomonas rein-hardtii, were investigated. We covalently immobilized CP12 on a resin and
then used it to trap CP12 partners. Thus, we found an association between
CP12 and phosphoribulokinase (EC 220.127.116.11), glyceraldehyde 3-phosphate
dehydrogenase (EC 18.104.22.168) and aldolase.
In animal cells, many proteins have been shown to undergo glutathionyla-tion under conditions of oxidative stress. By contrast, very little is known
about this post-translational modification in plants. In the present work,
we showed, using mass spectrometry, that the recombinant chloroplast
A4-glyceraldehyde-3-phosphate dehydrogenase (A4-GAPDH) from Arabid-opsis thaliana is glutathionylated with either oxidized glutathione or
reduced glutathione and H2O2.
he 8.5 kDa chloroplast protein CP12 is essential for assembly of the
phosphoribulokinase⁄glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
complex fromChlamydomonas reinhardtii. After reduction of this complex
with thioredoxin, phosphoribulokinase is released but CP12 remains tightly
associated with GAPDH and downregulates its NADPH-dependent activity.
A gene having high sequence homology (45–49%) with the glycerol-1-phosphate dehydrogenase gene from Methanobacterium thermoautotrophicum was cloned from the aerobic hyperthermophilic archaeon Aeropyrum pernix K1 (JCM 9820). This gene expressed in Escherichia coli with the pET vector system consists of 1113 nucleotides with an ATG initiation codon and a TAG termination codon. The molecular mass of the puriﬁed enzyme was estimated to be 38 kDa by SDS/PAGE and 72.4 kDa by gel column chromatography, indicating presence as a dimer....
We previously reported that GTS1 is involved in regulating ultradian oscillations of the glycolytic pathway induced by cyanide in cell suspensions as well as oscillations of energy metabolism in aerobic continuous cultures. Here, we screened a yeast cDNA library for proteins that bind to Gts1p using the yeast two-hybrid system and cloned multiple TDH cDNAs encoding the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH).
The involvement of the lysine residue present at the active site of Ehrlich ascites carcinoma (EAC) cell glyceraldehyde-3-phosphate dehydrogenase (Gra3P DH) was investigated by using the lysine speciﬁc reagents trinitrobenzenesulfonic acid (TNBS) and pyridoxal phosphate (PP). Both TNBS and PP inactivated EAC cell Gra3P DH with pseudo-ﬁrst-order kinetics with the rate dependent on modiﬁer concentration. Kinetic analysis, including a Tsou plot, indicated that both TNBS and PP apparently react with one lysine residue per enzyme molecule.
Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: Identification of Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a binding protein for a 68-kDa Bacillus thuringiensis parasporal protein cytotoxic against leukaemic cells
The glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
in the chloroplast ofChlamydomonas reinhardtiiis part of a
complex that also includes phosphoribulokinase (PRK) and
CP12. We identified two residues of GAPDH involved in
protein–protein interactions in this complex, by changing
residuesK128 andR197 intoAorE.K128A/Emutants had
aKmfor NADH that was twice that of the wild type and a
lower catalytic constant, whatever the cofactor.
We report here the first crystal structure of a stable isosteric
analogue of 1,3-bisphospho-D-glyceric acid (1,3-BPGA)
bound to the catalytic domain of Trypanosoma cruzi
glycosomal glyceraldehyde-3-phosphate dehydrogenase
(gGAPDH)in which the two phosphoryl moieties interact
with Arg249. This complex possibly illustrates a step of the
catalytic process by which Arg249 may induce compression
of the product formed, allowing its expulsion fromthe active
glyceraldehyde 3-phosphate dehydrogenase (GAPDH)
was purified from the green algaChlamydomonas reinhardtii
andwas alsooverexpressed inEscherichia coli. Bothpurified
A4 tetramers of recombinant and native GAPDH were
characterized for the first time. The pH optimum for both
nativeandrecombinant enzymeswas close to7.8.ThepKsof
theresidues involvedincatalysis indicate thatacysteineanda
histidinemay take part in catalysis by chloroplast GAPDH,
as is the case for glycolytic GAPDH.
Bối cảnh: Thiếu Glucose-6-phosphatase dehydrogenase (G-6-PD) là bệnh lý về men thường gặp nhất ở người. Di truyền theo nhiễm sắc thể X, thiếu G6PD gây bệnh cho khoảng 400 triệu người trên thế giới. Bệnh rất đa dạng với hơn 300 biến thể đã được báo cáo. Bệnh mang lại sự bảo vệ chống sốt rét có thể do tần số gen cao của nó.
Dehydrogenase (G6PDH) là một enzyme có chức năng bảo vệ màng hồng cầu (HC) và duy trì tuổi thọ bình thường cho hồng cầu. Thiếu men G6PDH là một bệnh lý hay nói đúng hơn là một khiếm khuyết của màng hồng cầu ở người và có di truyền liên kết giới tính X, và khoảng 400 triệu người trên toàn cầu đang mắc khiếm khuyết này với hơn 400 biến thể đa dạng khác nhau. Khi thiếu men này có thể gây ra các bệnh lý tán huyết trên lâm sàng khi người đó phơi nhiễm hoặc gặp...
ATP and ADP inhibit, in varying degrees, several dehydrogenases of the
central carbon metabolism of Lactococcus lactisATCC 19435in vitro, i.e.
glyceraldehyde-3-phosphate dehydrogenase (GAPDH), lactate dehydroge-nase (LDH) and alcohol dehydrogenase (ADH). Here we demonstrate
mixed inhibition for GAPDH and competitive inhibition for LDH and
ADH by adenine nucleotides in single inhibition studies.