グリセルアルデヒド3リン酸脱水素酵素

関: G3PD、GAPD、GAPDH、glyceraldehyde-3-phosphate dehydrogenase

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/02/11 15:18:17」(JST)

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Glyceraldehyde 3-phosphate dehydrogenase, C-terminal domain

crystal structure of glyceraldehyde-3-phosphate dehydrogenase from pyrococcus horikoshii ot3

Identifiers

Symbol

Gp_dh_C

Pfam

PF02800

Pfam clan

CL0139

InterPro

IPR020829

PROSITE

PDOC00069

SCOP

1gd1

SUPERFAMILY

1gd1

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Glyceraldehyde 3-phosphate dehydrogenase (abbreviated as GAPDH or less commonly as G3PDH) (EC 1.2.1.12) is an enzyme of ~37kDa that catalyzes the sixth step of glycolysis and thus serves to break down glucose for energy and carbon molecules. In addition to this long established metabolic function, GAPDH has recently been implicated in several non-metabolic processes, including transcription activation, initiation of apoptosis,^[1] ER to Golgi vesicle shuttling, and fast axonal, or axoplasmic transport.^[2] In sperm, a testis-specific isoenzyme GAPDHS takes its role.

1 Metabolic function
- 1.1 Overall reaction catalyzed
- 1.2 Two-step conversion of glyceraldehyde-3-phosphate
- 1.3 Mechanism of catalysis
- 1.4 Enzyme regulation
- 1.5 Interactive pathway map
2 Additional functions
- 2.1 Transcription and apoptosis
3 Metabolic switch
- 3.1 ER to Golgi transport
4 Cellular location
5 Usage of GAPDH as loading control
6 References
7 Further reading

Metabolic function

As its name indicates, glyceraldehyde 3-phosphate dehydrogenase (GAPDH) catalyses the conversion of glyceraldehyde 3-phosphate to D-glycerate 1,3-bisphosphate. This is the 6th step in the glycolytic breakdown of glucose, an important pathway of energy and carbon molecule supply which takes place in the cytosol of eukaryotic cells. The conversion occurs in two coupled steps. The first is favourable and allows the second unfavourable step to occur.

Overall reaction catalyzed

glyceraldehyde 3-phosphate	glyceraldehyde phosphate dehydrogenase		D-glycerate 1,3-bisphosphate

	NAD⁺ +P_i	NADH + H⁺

	NAD⁺ +P_i	NADH + H⁺

Compound C00118 at KEGG Pathway Database. Enzyme 1.2.1.12 at KEGG Pathway Database. Reaction R01063 at KEGG Pathway Database. Compound C00236 at KEGG Pathway Database.

Two-step conversion of glyceraldehyde-3-phosphate

The first reaction is the oxidation of glyceraldehyde 3-phosphate at the carbon 1 position (in the diagram it is shown as the 4th carbon from glycolysis), in which an aldehyde is converted into a carboxylic acid (ΔG°'=-50 kJ/mol (-12kcal/mol)) and NAD+ is simultaneously reduced endergonically to NADH.

The energy released by this highly exergonic oxidation reaction drives the endergonic second reaction (ΔG°'=+50 kJ/mol (+12kcal/mol)), in which a molecule of inorganic phosphate is transferred to the GAP intermediate to form a product with high phosphoryl-transfer potential: 1,3-bisphosphoglycerate (1,3-BPG).

This is an example of phosphorylation coupled to oxidation, and the overall reaction is somewhat endergonic (ΔG°'=+6.3 kJ/mol (+1.5)). Energy coupling here is made possible by GAPDH.

Mechanism of catalysis

GAPDH uses covalent catalysis and general base catalysis to decrease the very large and positive activation energy of the second step of this reaction. First, a cysteine residue in the active site of GAPDH attacks the carbonyl group of GAP, creating a hemithioacetal intermediate (covalent catalysis). Next, an adjacent, tightly bound molecule of NAD⁺ accepts a hydride ion from GAP, forming NADH; GAP is concomitantly oxidized to a thioester intermediate using a molecule of water. This thioester species is much higher in energy than the carboxylic acid species that would result in the absence of GAPDH (the carboxylic acid species is so low in energy that the energy barrier for the second step of the reaction (phosphorylation) would be too high, and the reaction, therefore, too slow and equilibrium too unfavorable for a living organism). Donation of the hydride ion by the hemithioacetal is facilitated by its deprotonation by a histidine residue in the enzyme's active site (general base catalysis). Deprotonation encourages the reformation of the carbonyl group in the thioester intermediate and ejection of the hydride ion. NADH leaves the active site and is replaced by another molecule of NAD⁺, the positive charge of which stabilizes the negatively charged carbonyl oxygen in the transition state of the next and ultimate step. Finally, a molecule of inorganic phosphate attacks the thioester and forms a tetrahedral intermediate, which then collapses to release 1,3-bisphosphoglycerate, and the thiol group of the enzyme's cysteine residue.

Enzyme regulation

This protein may use the morpheein model of allosteric regulation.^[3]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^{[§ 1]}

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|{{{bSize}}}px|alt=Glycolysis and Gluconeogenesis edit|]]

File:WP534.png

Glycolysis and Gluconeogenesis edit

^ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

Additional functions

GAPDH, like many other enzymes, has multiple functions. In addition to catalysing the 6th step of glycolysis, recent evidence implicates GAPDH in other cellular processes. This came as a surprise to researchers but it makes evolutionary sense to re-use and adapt existing proteins instead of evolving a novel protein from scratch.

GAPDH can also be inhibited by arsenate, inhibiting glycolysis in red blood cells and causing hemolytic anemia.

Transcription and apoptosis

GAPDH can itself activate transcription. The OCA-S transcriptional coactivator complex contains GAPDH and lactate dehydrogenase, two proteins previously only thought to be involved in metabolism. GAPDH moves between the cytosol and the nucleus and may thus link the metabolic state to gene transcription.^[4]

In 2005, Hara et al. showed that GAPDH initiates apoptosis. This is not a third function, but can be seen as an activity mediated by GAPDH binding to DNA like in transcription activation, discussed above. The study demonstrated that GAPDH is S-nitrosylated by NO in response to cell stress, which causes it to bind to the protein SIAH1, a ubiquitin ligase. The complex moves into the nucleus where Siah1 targets nuclear proteins for degradation, thus initiating controlled cell shutdown.^[5] In subsequent study the group demonstrated that deprenyl, which has been used clinically to treat Parkinson's disease, strongly reduces the apoptotic action of GAPDH by preventing its S-nitrosylation and might thus be used as a drug.^[6]

Metabolic switch

GAPDH acts as reversible metabolic switch under oxidative stress.^[7] When cells are exposed to oxidants, they need excessive amounts of the antioxidant cofactor NADPH. In the cytosol, NADPH is reduced from NADP+ by several enzymes, three of them catalyze the first steps of the Pentose phosphate pathway. Oxidant-treatments cause an inactivation of GAPDH. This inactivation re-routes temporally the metabolic flux from glycolysis to the Pentose Phosphate Pathway, allowing the cell to generate more NADPH.^[8] Under stress conditions, NADPH is needed by some antioxidant-systems including glutaredoxin and thioredoxin as well as being essential for the recycling of gluthathione.

ER to Golgi transport

GAPDH also appears to be involved in the vesicle transport from the endoplasmic reticulum (ER) to the Golgi apparatus which is part of shipping route for secreted proteins. It was found that GAPDH is recruited by rab2 to the vesicular-tubular clusters of the ER where it helps to form COP 1 vesicles. GAPDH is activated via tyrosine phosphorylation by Src.^[9]

Cellular location

All steps of glycolysis take place in the cytosol and so does the reaction catalysed by GAPDH. Research in red blood cells indicates that GAPDH and several other glycolytic enzymes assemble in complexes on the inside of the cell membrane. The process appears to be regulated by phosphorylation and oxygenation.^[10] Bringing several glycolytic enzymes close to each other is expected to greatly increase the overall speed of glucose breakdown.

Usage of GAPDH as loading control

Because the GAPDH gene is often stably and constitutively expressed at high levels in most tissues and cells, it is considered a housekeeping gene. For this reason, GAPDH is commonly used by biological researchers as a loading control for western blot and as a control for qPCR. However, researchers have reported different regulation of GAPDH under specific conditions.^[11] For example, the transcription factor MZF-1 has been shown to regulate the GAPDH gene.^[12] Therefore, the use of GAPDH as loading control has to be considered carefully.

References

^ Tarze A, Deniaud A, Le Bras M, Maillier E, Molle D, Larochette N, Zamzami N, Jan G, Kroemer G, Brenner C (April 2007). "GAPDH, a novel regulator of the pro-apoptotic mitochondrial membrane permeabilization". Oncogene 26 (18): 2606–20. doi:10.1038/sj.onc.1210074. PMID 17072346.
^ Zala D, Hinckelmann MV, Yu H, Lyra da Cunha MM, Liot G, Cordelières FP, Marco S, Saudou F (January 2013). "Vesicular glycolysis provides on-board energy for fast axonal transport". Cell 152 (3): 479–91. doi:10.1016/j.cell.2012.12.029. PMID 23374344.
^ Selwood T, Jaffe EK (March 2012). "Dynamic dissociating homo-oligomers and the control of protein function". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.
^ Zheng L, Roeder RG, Luo Y (2003). "S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component". Cell 114 (2): 255–66. doi:10.1016/S0092-8674(03)00552-X. PMID 12887926.
^ Hara MR, Agrawal N, Kim SF, Cascio MB, Fujimuro M, Ozeki Y, Takahashi M, Cheah JH, Tankou SK, Hester LD, Ferris CD, Hayward SD, Snyder SH, Sawa A (July 2005). "S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding". Nat. Cell Biol. 7 (7): 665–74. doi:10.1038/ncb1268. PMID 15951807.
^ Hara MR, Thomas B, Cascio MB, Bae BI, Hester LD, Dawson VL, Dawson TM, Sawa A, Snyder SH (March 2006). "Neuroprotection by pharmacologic blockade of the GAPDH death cascade". Proc. Natl. Acad. Sci. U.S.A. 103 (10): 3887–9. doi:10.1073/pnas.0511321103. PMC 1450161. PMID 16505364.
^ Agarwal AR, Zhao L, Sancheti H, Sundar IK, Rahman I, Cadenas E. "Short-term cigarette smoke exposure induces reversible changes in energy metabolism and cellular redox status independent of inflammatory responses in mouse lungs". Am J Physiol Lung Cell Mol Physiol 10: L889-98 year = 2012. doi:10.1152/ajplung. PMID 23064950.
^ Ralser M, Wamelink MM, Kowald A, Gerisch B, Heeren G, Struys EA, Klipp E, Jakobs C, Breitenbach M, Lehrach H, Krobitsch S (2007). "Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress". J. Biol. 6 (4): 10. doi:10.1186/jbiol61. PMC 2373902. PMID 18154684.
^ Tisdale EJ, Artalejo CR (June 2007). "A GAPDH mutant defective in Src-dependent tyrosine phosphorylation impedes Rab2-mediated events". Traffic 8 (6): 733–41. doi:10.1111/j.1600-0854.2007.00569.x. PMID 17488287.
^ Campanella ME, Chu H, Low PS (February 2005). "Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane". Proc. Natl. Acad. Sci. U.S.A. 102 (7): 2402–7. doi:10.1073/pnas.0409741102. PMC 549020. PMID 15701694.
^ Barber RD, Harmer DW, Coleman RA, Clark BJ (May 2005). "GAPDH as a housekeeping gene: analysis of GAPDH mRNA expression in a panel of 72 human tissues". Physiol. Genomics 21 (3): 389–95. doi:10.1152/physiolgenomics.00025.2005. PMID 15769908.
^ Piszczatowski RT, Rafferty BJ, Rozado A, Tobak S, Lents NH (15 August 2014). "The glyceraldehyde 3-phosphate dehydrogenase gene (GAPDH) is regulated by myeloid zinc finger 1 (MZF-1) and is induced by calcitriol". Biochemical and Biophysical Research Communications 451 (1): 137-141. doi:10.1016/j.bbrc.2014.07.082. PMID 25065746.

English Journal

Biochemical characterisation of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) from the liver fluke, Fasciola hepatica.

Zinsser VL1, Hoey EM1, Trudgett A1, Timson DJ2.Author information 1School of Biological Sciences, Queen's University Belfast, Medical Biology Centre, 97 Lisburn Road, Belfast BT9 7BL, UK.2School of Biological Sciences, Queen's University Belfast, Medical Biology Centre, 97 Lisburn Road, Belfast BT9 7BL, UK. Electronic address: d.timson@qub.ac.uk.AbstractGlyceraldehyde 3-phosphate dehydrogenase (GAPDH) catalyses one of the two steps in glycolysis which generate the reduced coenzyme NADH. This reaction precedes the two ATP generating steps. Thus, inhibition of GAPDH will lead to substantially reduced energy generation. Consequently, there has been considerable interest in developing GAPDH inhibitors as anti-cancer and anti-parasitic agents. Here, we describe the biochemical characterisation of GAPDH from the common liver fluke Fasciola hepatica (FhGAPDH). The primary sequence of FhGAPDH is similar to that from other trematodes and the predicted structure shows high similarity to those from other animals including the mammalian hosts. FhGAPDH lacks a binding pocket which has been exploited in the design of novel antitrypanosomal compounds. The protein can be expressed in, and purified from Escherichia coli; the recombinant protein was active and showed no cooperativity towards glyceraldehyde 3-phosphate as a substrate. In the absence of ligands, FhGAPDH was a mixture of homodimers and tetramers, as judged by protein-protein crosslinking and analytical gel filtration. The addition of either NAD+ or glyceraldehyde 3-phosphate shifted this equilibrium towards a compact dimer. Thermal scanning fluorimetry demonstrated that this form was considerably more stable than the unliganded one. These responses to ligand binding differ from those seen in mammalian enzymes. These differences could be exploited in the discovery of reagents which selectively disrupt the function of FhGAPDH.
Biochimica et biophysica acta.Biochim Biophys Acta.2014 Feb 22. pii: S1570-9639(14)00029-6. doi: 10.1016/j.bbapap.2014.02.008. [Epub ahead of print]
Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) catalyses one of the two steps in glycolysis which generate the reduced coenzyme NADH. This reaction precedes the two ATP generating steps. Thus, inhibition of GAPDH will lead to substantially reduced energy generation. Consequently, there has been co
PMID 24566472

Morphological and phylogenetic identification of Botrytis sinoviticola, a novel cryptic species causing gray mold disease on table grapes (Vitis vinifera) in China.

Zhou Y1, Zhang J, Wang X, Yang L, Jiang DH, Li GQ, Hsiang T, Zhuang WY.Author information 1Huazhong Agricultural University, wuhan, hubei, China.AbstractSeventy-five isolates of Botrytis collected from table grapes (Vitis vinifera) showing gray mold symptoms in China were identified based on morpho-cultural characteristics on potato dextrose agar (20 C) and/or phylogenetic analysis using the sequences of three nuclear genes (G3PDH, HSP60, RPB2). Isolates of different species of Botrytis were compared using fenhexamid sensitivity, Bc-hch gene-RFLP haplotyping and pathogenicity on table grapes. The 75 isolates were found to comprise two species: B. cinerea (63 isolates) and Botrytis sp. (12 isolates). Botrytis sp. is a novel species described here as Botrytis sinoviticola Zhang et al. sp. nov. Both B. sinoviticola (Bs) and B. cinerea (Bc) were found to have optimum temperatures at 20 C for mycelial growth and at 25 C for conidial germination. Sensitivity to fenhexamid was significantly greater (P < 0.05) for Bc (EC50 = 0.04-0.01 µg mL-1) than for Bs (EC50 = 0.08-0.02 µg mL-1). Digestion of the PCR-amplicons of the Bc-hch gene with Hha I generated two haplotypes, namely Group I haplotype for Bs and Group II haplotype for Bc. Bs infected table grapes (leaves, berries) only through wounds, whereas Bc infected both injured and non-injured tissues of table grapes. This study suggests that Bs is a cryptic species sympatric with Bc on table grapes in China.
Mycologia.Mycologia.2014 Jan 6. [Epub ahead of print]
Seventy-five isolates of Botrytis collected from table grapes (Vitis vinifera) showing gray mold symptoms in China were identified based on morpho-cultural characteristics on potato dextrose agar (20 C) and/or phylogenetic analysis using the sequences of three nuclear genes (G3PDH, HSP60, RPB2). Iso
PMID 24396103

Characterization of two mitochondrial flavin adenine dinucleotide-dependent glycerol-3-phosphate dehydrogenases in Trypanosoma brucei.

Škodová I1, Verner Z, Bringaud F, Fabian P, Lukeš J, Horváth A.Author information 1Department of Biochemistry, Comenius University, Bratislava, Slovakia.AbstractGlycerol-3-phosphate dehydrogenases (G3PDHs) constitute a shuttle that serves for regeneration of NAD(+) reduced during glycolysis. This NAD-dependent enzyme is employed in glycolysis and produces glycerol-3-phosphate from dihydroxyacetone phosphate, while its flavin adenine dinucleotide (FAD)-dependent homologue catalyzes a reverse reaction coupled to the respiratory chain. Trypanosoma brucei possesses two FAD-dependent G3PDHs. While one of them (mitochondrial G3PDH [mtG3PDH]) has been attributed to the mitochondrion and seems to be directly involved in G3PDH shuttle reactions, the function of the other enzyme (putative G3PDH [putG3PDH]) remains unknown. In this work, we used RNA interference and protein overexpression and tagging to shed light on the relative contributions of both FAD-G3PDHs to overall cellular metabolism. Our results indicate that mtG3PDH is essential for the bloodstream stage of T. brucei, while in the procyclic stage the enzyme is dispensable. Expressed putG3PDH-V5 was localized to the mitochondrion, and the data obtained by digitonin permeabilization, Western blot analysis, and immunofluorescence indicate that putG3PDH is located within the mitochondrion.
Eukaryotic cell.Eukaryot Cell.2013 Dec;12(12):1664-73. doi: 10.1128/EC.00152-13. Epub 2013 Oct 18.
Glycerol-3-phosphate dehydrogenases (G3PDHs) constitute a shuttle that serves for regeneration of NAD(+) reduced during glycolysis. This NAD-dependent enzyme is employed in glycolysis and produces glycerol-3-phosphate from dihydroxyacetone phosphate, while its flavin adenine dinucleotide (FAD)-depen
PMID 24142106

Japanese Journal

Appearance of a new leaf rot disease on common ice plant

MAEDA Kazuyuki,KURAHASHI Yoshio,OHSATO Shuichi,YONEYAMA Katsuyoshi
Journal of general plant pathology : JGPP 76(5), 303-309, 2010-10-01
NAID 10029719952

プロポリス由来3,4,5-トリカフェオイルキナ酸による神経細胞保護作用

韓〓奎,礒田博子,繁森英幸 [他],寺川美加
バイオサイエンスとインダストリー = Bioscience & industry 68(3), 203-205, 2010-05-01
NAID 10026195170

Amount of Ribulose-1, 5-bisphosphate Carboxylase/Oxygenase (Rubisco) Protein and Levels of mRNAs of rbcS and rbcL in the Leaves at Different Positions in Transgenic Rice Plants with Decreased Content of Rubisco(Plant Nutrition)

Ishizuka Michio,Makino Amane,Suzuki Yuji [他],Mae Tadahiko
Soil science and plant nutrition 50(2), 233-239, 2004-04-00
… The differences in the amounts of various photosynthetic components, including ribulose-1, 5-bisphosphate carboxylase/oxygenase (Rubisco) and chlorophyll (Chl), and the activities of chloroplastic fructose-1, 6-bisphosphatase (Cp-FBPase), NADP-glyceraldehyde-3-phosphate dehydrogenase (NADP-G3PDH), ribulose-5-phosphate kinase (Ru5P kinase), and sucrose-phosphate synthase (SPS) enzymes were examined in leaf blades at different leaf positions on the main culms of transgenic rbcS antisense rice plants. …
NAID 110001720283

「GAPD」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Glyceraldehyde 3-phosphate dehydrogenase, NAD binding domain
	determinants of enzyme thermostability observed in the molecular structure of thermus aquaticus d-glyceraldehyde-3-phosphate dehydrogenase at 2.5 angstroms resolution
Identifiers
Symbol	Gp_dh_N
Pfam	PF00044
Pfam clan	CL0063
InterPro	IPR020828
PROSITE	PDOC00069
SCOP	1gd1
SUPERFAMILY	1gd1
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Glyceraldehyde-3-phosphate dehydrogenase
	; GAPDH with NAD+ and Pi bound to the active site. PDB rendering based on 2CZC.
Available structures
PDB	Ortholog search: PDBe, RCSB
List of PDB id codes
	1U8F, 1ZNQ, 2FEH, 3GPD
Identifiers
Symbols	GAPDH ; G3PD; GAPD; HEL-S-162eP
External IDs	OMIM: 138400 MGI: 3646088 HomoloGene: 107053 ChEMBL: 2284 GeneCards: GAPDH Gene
EC number	1.2.1.12
Gene ontology
Molecular function	• glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; • protein binding; • microtubule binding; • peptidyl-cysteine S-nitrosylase activity; • identical protein binding; • NADP binding; • NAD binding;
Cellular component	• nucleus; • cytoplasm; • lipid particle; • cytosol; • plasma membrane; • microtubule cytoskeleton; • membrane; • ribonucleoprotein complex; • perinuclear region of cytoplasm; • extracellular vesicular exosome; • GAIT complex;
Biological process	• microtubule cytoskeleton organization; • carbohydrate metabolic process; • glucose metabolic process; • gluconeogenesis; • glycolytic process; • negative regulation of translation; • peptidyl-cysteine S-trans-nitrosylation; • small molecule metabolic process; • protein stabilization; • neuron apoptotic process; • oxidation-reduction process; • cellular response to interferon-gamma;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	This box: view; talk; edit;

　　[★]

グリセルアルデヒド3リン酸脱水素酵素

関: G3PD、G3PDH、GAPDH、glyceraldehyde-3-phosphate dehydrogenase

「G3PD」

　　[★]

グリセルアルデヒド3リン酸脱水素酵素

関: G3PDH、GAPD、GAPDH、glyceraldehyde-3-phosphate dehydrogenase

[WikiPathways-4] The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

[pmid17072346-1] Tarze A, Deniaud A, Le Bras M, Maillier E, Molle D, Larochette N, Zamzami N, Jan G, Kroemer G, Brenner C (April 2007). "GAPDH, a novel regulator of the pro-apoptotic mitochondrial membrane permeabilization". Oncogene 26 (18): 2606–20. doi:10.1038/sj.onc.1210074. PMID 17072346.

[pmid23374344-2] Zala D, Hinckelmann MV, Yu H, Lyra da Cunha MM, Liot G, Cordelières FP, Marco S, Saudou F (January 2013). "Vesicular glycolysis provides on-board energy for fast axonal transport". Cell 152 (3): 479–91. doi:10.1016/j.cell.2012.12.029. PMID 23374344.

[pmid22182754-3] Selwood T, Jaffe EK (March 2012). "Dynamic dissociating homo-oligomers and the control of protein function". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.

[pmid12887926-5] Zheng L, Roeder RG, Luo Y (2003). "S phase activation of the histone H2B promoter by OCA-S, a coactivator complex that contains GAPDH as a key component". Cell 114 (2): 255–66. doi:10.1016/S0092-8674(03)00552-X. PMID 12887926.

[pmid15951807-6] Hara MR, Agrawal N, Kim SF, Cascio MB, Fujimuro M, Ozeki Y, Takahashi M, Cheah JH, Tankou SK, Hester LD, Ferris CD, Hayward SD, Snyder SH, Sawa A (July 2005). "S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding". Nat. Cell Biol. 7 (7): 665–74. doi:10.1038/ncb1268. PMID 15951807.

[pmid16505364-7] Hara MR, Thomas B, Cascio MB, Bae BI, Hester LD, Dawson VL, Dawson TM, Sawa A, Snyder SH (March 2006). "Neuroprotection by pharmacologic blockade of the GAPDH death cascade". Proc. Natl. Acad. Sci. U.S.A. 103 (10): 3887–9. doi:10.1073/pnas.0511321103. PMC 1450161. PMID 16505364.

[pmid23064950-8] Agarwal AR, Zhao L, Sancheti H, Sundar IK, Rahman I, Cadenas E. "Short-term cigarette smoke exposure induces reversible changes in energy metabolism and cellular redox status independent of inflammatory responses in mouse lungs". Am J Physiol Lung Cell Mol Physiol 10: L889-98 year = 2012. doi:10.1152/ajplung. PMID 23064950.

[pmid18154684-9] Ralser M, Wamelink MM, Kowald A, Gerisch B, Heeren G, Struys EA, Klipp E, Jakobs C, Breitenbach M, Lehrach H, Krobitsch S (2007). "Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress". J. Biol. 6 (4): 10. doi:10.1186/jbiol61. PMC 2373902. PMID 18154684.

[pmid17488287-10] Tisdale EJ, Artalejo CR (June 2007). "A GAPDH mutant defective in Src-dependent tyrosine phosphorylation impedes Rab2-mediated events". Traffic 8 (6): 733–41. doi:10.1111/j.1600-0854.2007.00569.x. PMID 17488287.

[pmid15701694-11] Campanella ME, Chu H, Low PS (February 2005). "Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane". Proc. Natl. Acad. Sci. U.S.A. 102 (7): 2402–7. doi:10.1073/pnas.0409741102. PMC 549020. PMID 15701694.

[pmid15769908-12] Barber RD, Harmer DW, Coleman RA, Clark BJ (May 2005). "GAPDH as a housekeeping gene: analysis of GAPDH mRNA expression in a panel of 72 human tissues". Physiol. Genomics 21 (3): 389–95. doi:10.1152/physiolgenomics.00025.2005. PMID 15769908.

[13] Piszczatowski RT, Rafferty BJ, Rozado A, Tobak S, Lents NH (15 August 2014). "The glyceraldehyde 3-phosphate dehydrogenase gene (GAPDH) is regulated by myeloid zinc finger 1 (MZF-1) and is induced by calcitriol". Biochemical and Biophysical Research Communications 451 (1): 137-141. doi:10.1016/j.bbrc.2014.07.082. PMID 25065746.

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案内

案内

G3PDH