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transaldolase 1
Identifiers
Symbol	TALDO1
Entrez	6888
HUGO	11559
OMIM	602063
RefSeq	NM_006755
UniProt	P37837
Other data
EC number	2.2.1.2
Locus	Chr. 11 p15.5-15.4

transaldolase B
Identifiers
Symbol	talB
Entrez	4199095
PDB	1onr
RefSeq	NC_008245.1
UniProt	P0A870
Other data
EC number	2.2.1.2

Transaldolase is an enzyme (EC 2.2.1.2) of the non-oxidative phase of the pentose phosphate pathway. In humans, transaldolase is encoded by the TALDO1 gene.^[3]^[4]

The following chemical reaction is catalyzed by transaldolase:

sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate erythrose 4-phosphate + fructose 6-phosphate

Clinical significance

The pentose phosphate pathway has two metabolic functions: (1) generation of nicotinamide adenine dinucleotide phosphate (reduced NADPH), for reductive biosynthesis, and (2) formation of ribose, which is an essential component of ATP, DNA, and RNA. Transaldolase links the pentose phosphate pathway to glycolysis. In patients with deficiency of transaldolase, there's an accumulation of erythritol (from erythrose 4-phosphate), D-arabitol, and ribitol.^[5]^[6]

The deletion in 3 base pairs in the TALDO1 gene results in the absence of serine at position 171 of the transaldolase protein, which is part of a highly conserved region, suggesting that the mutation causes the transaldolase deficiency that is found in erythrocytes and lymphoblasts.^[5] The deletion of this amino acid can lead to liver cirrhosis and hepatosplenomegaly (enlarged spleen and liver) during early infancy. Transaldolase is also a target of autoimmunity in patients with multiple sclerosis.^[7]

Structure

Active site of the transaldolase enzyme highlighting the key amino acid residues (Asp-27, Glu-106, and Lys-142) involved in catalysis.^[1]

Transaldolase is a single domain composed of 337 amino acids. The core structure is an α/β barrel, similar to other class I aldolases, made up of eight parallel β-sheets and seven α-helices. There are also seven additional α-helices that are not part of the barrel. Hydrophobic amino acids are located between the β-sheets in the barrel and the surrounding α-helices to contribute to packing, such as the area containing Leu-168, Phe-170, Phe-189, Gly-311, and Phe-315. In the crystal, human transaldolase forms a dimer, with the two subunits connected by 18 residues in each subunit. See mechanism to the left for details.

The active site, located in the center of the barrel, contains three key residues: lysine-142, glutamate-106, and aspartate-27. The lysine holds the sugar in place while the glutamate and aspartate act as proton donors and acceptors.^[1]

Mechanism of catalysis

The residue of lysine-142 in the active site of transaldolase forms a Schiff base with the keto group in sedoheptulose-7-phosphate after deprotonation by another active site residue, glutamate-106. The reaction mechanism is similar to the reverse reaction catalyzed by aldolase: The bond joining carbons 3 and 4 is broken, leaving dihydroxyacetone joined to the enzyme via a Schiff base. This cleavage reaction generates the unusual aldose sugar erythrose-4-phosphate. Then transaldolase catalyzes the condensation of glyceraldehyde-3-phosphate with the Schiff base of dihydroxyacetone, yielding enzyme-bound fructose 6-phosphate. Hydrolysis of the Schiff base liberates free fructose 6-phosphate, one of the products of the pentose phosphate pathway.

Reaction scheme for the conversion of sedoheptulose-7-phosphate to fructose-6-phosphate.^[8]

The pentose phosphate pathway adapted from (Verhoeven, 2001)^[5]

References

^ ^a ^b ^c PDB: 1F05; Thorell S, Gergely P, Banki K, Perl A, Schneider G (June 2000). "The three-dimensional structure of human transaldolase". FEBS Lett. 475 (3): 205–8. doi:10.1016/S0014-5793(00)01658-6. PMID 10869557.
^ Molecular graphics images were produced using the UCSF Chimera package from the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco. Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE (October 2004). "UCSF Chimera–a visualization system for exploratory research and analysis". J Comput Chem 25 (13): 1605–12. doi:10.1002/jcc.20084. PMID 15264254.
^ "Entrez Gene: transaldolase 1".
^ Banki K, Eddy RL, Shows TB, Halladay DL, Bullrich F, Croce CM, Jurecic V, Baldini A, Perl A (October 1997). "The human transaldolase gene (TALDO1) is located on chromosome 11 at p15.4-p15.5". Genomics 45 (1): 233–8. doi:10.1006/geno.1997.4932. PMID 9339383.
^ ^a ^b ^c Verhoeven NM, Huck JH, Roos B, Struys EA, Salomons GS, Douwes AC, van der Knaap MS, Jakobs C (May 2001). "Transaldolase deficiency: liver cirrhosis associated with a new inborn error in the pentose phosphate pathway". Am. J. Hum. Genet. 68 (5): 1086–92. doi:10.1086/320108. PMC 1226089. PMID 11283793.
^ Perl A (June 2007). "The pathogenesis of transaldolase deficiency". IUBMB Life 59 (6): 365–73. doi:10.1080/15216540701387188. PMID 17613166.
^ Niland B, Perl A (2004). "Evaluation of autoimmunity to transaldolase in multiple sclerosis". Methods Mol. Med. 102: 155–71. doi:10.1385/1-59259-805-6:155. PMID 15286385.
^ Jia J, Schörken U, Lindqvist Y, Sprenger GA, Schneider G (January 1997). "Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases". Protein Sci. 6 (1): 119–24. doi:10.1002/pro.5560060113. PMC 2143518. PMID 9007983.

External links

Transaldolase at the US National Library of Medicine Medical Subject Headings (MeSH)

UpToDate Contents

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1. 先天性代謝異常：疫学、病因、および臨床的特徴 inborn errors of metabolism epidemiology pathogenesis and clinical features
2. 先天性代謝異常：代謝性救急疾患 inborn errors of metabolism metabolic emergencies

English Journal

PHO13 deletion-induced transcriptional activation prevents sedoheptulose accumulation during xylose metabolism in engineered Saccharomyces cerevisiae.

Xu H1, Kim S2, Sorek H3, Lee Y4, Jeong D4, Kim J2, Oh EJ1, Yun EJ2, Wemmer DE3, Kim KH2, Kim SR5, Jin YS6.
Metabolic engineering.Metab Eng.2016 Mar;34:88-96. doi: 10.1016/j.ymben.2015.12.007. Epub 2015 Dec 25.
The deletion of PHO13 (pho13Δ) in Saccharomyces cerevisiae, encoding a phosphatase enzyme of unknown specificity, results in the transcriptional activation of genes related to the pentose phosphate pathway (PPP) such as TAL1 encoding transaldolase. It has been also reported that the pho13Δ mutant
PMID 26724864

Proteomics analysis of high lipid-producing strain Mucor circinelloides WJ11: an explanation for the mechanism of lipid accumulation at the proteomic level.

Tang X1, Zan X2, Zhao L3, Chen H4,5, Chen YQ6,7, Chen W8,9, Song Y10,11, Ratledge C12.
Microbial cell factories.Microb Cell Fact.2016 Feb 11;15(1):35. doi: 10.1186/s12934-016-0428-4.
BACKGROUND: The oleaginous fungus, Mucor circinelloides, is attracting considerable interest as it produces oil rich in γ-linolenic acid. Nitrogen (N) deficiency is a common strategy to trigger the lipid accumulation in oleaginous microorganisms. Although a simple pathway from N depletion in the me
PMID 26867592

Complex coordinated extracellular metabolism: Acid phosphatases activate diluted human leukocyte proteins to generate energy flow as NADPH from purine nucleotide ribose.

Hibbs JB Jr1, Vavrin Z2, Cox JE3.
Redox biology.Redox Biol.2016 Feb 2;8:271-284. doi: 10.1016/j.redox.2016.02.001. [Epub ahead of print]
Complex metabolism is thought to occur exclusively in the crowded intracellular environment. Here we report that diluted enzymes from lysed human leukocytes produce extracellular energy. Our findings involve two pathways: the purine nucleotide catabolic pathway and the pentose phosphate pathway, whi
PMID 26895212

Japanese Journal

Two transaldolase isogenes from Moniliella megachiliensis behave in a different way depending on the stress class(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)

Iwata Hisashi,Mizushima Daiki,Kobayashi Yosuke [他],Ookura Tetsuya,Ogihara Jun,Kato Jun,Kasumi Takafumi
Journal of bioscience and bioengineering 119(2), 148-152, 2015-02
… We cloned and sequenced two transaldolase genes from Moniliella megachiliensis, a microorganism known to produce a significant amount of erythritol under hyper-osmotic stress. …
NAID 110009922497

1P-163 Pichia pastorisのメタノール代謝におけるキシルロース-5 リン酸供給系の機能と役割の解明(代謝工学,一般講演)

福岳寛隆,早川享志,中川智行
日本生物工学会大会講演要旨集 66, 58, 2014-08-05
NAID 110009906244

Co-expression of TAL1 and ADH1 in recombinant xylose-fermenting Saccharomyces cerevisiae improves ethanol production from lignocellulosic hydrolysates in the presence of furfural(MICROBIAL PHYSIOLOGY AND BIOTECHNOLOGY)

Hasunuma Tomohisa,Ismail Ku Syahidah Ku,Nambu Yumiko [他],Kondo Akihiko
Journal of bioscience and bioengineering 117(2), 165-169, 2014-02
… Under the synergistic conditions of transaldolase (TAL) and alcohol dehydrogenase (ADH) overexpression, S. …
NAID 110009804067

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Transaldolase
	Crystallographic structure of human transaldolase.
Identifiers
Symbol	Transaldolase
Pfam	PF00923
InterPro	IPR001585
PROSITE	PDOC00741
SCOP	1ucw
SUPERFAMILY	1ucw
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Search
PMC	articles
PubMed	articles
NCBI	proteins

Transaldolase
Identifiers
EC number	2.2.1.2
CAS number	9014-46-4
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins

　　[★]

英: [[]]
同: transaldolase
関: [[]]

-transaldolase

同: transaldolase

[pmid10869557-1] PDB: 1F05; Thorell S, Gergely P, Banki K, Perl A, Schneider G (June 2000). "The three-dimensional structure of human transaldolase". FEBS Lett. 475 (3): 205–8. doi:10.1016/S0014-5793(00)01658-6. PMID 10869557.

[pmid15264254-2] Molecular graphics images were produced using the UCSF Chimera package from the Resource for Biocomputing, Visualization, and Informatics at the University of California, San Francisco. Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE (October 2004). "UCSF Chimera–a visualization system for exploratory research and analysis". J Comput Chem 25 (13): 1605–12. doi:10.1002/jcc.20084. PMID 15264254.

[entrez-3] "Entrez Gene: transaldolase 1".

[pmid9339383-4] Banki K, Eddy RL, Shows TB, Halladay DL, Bullrich F, Croce CM, Jurecic V, Baldini A, Perl A (October 1997). "The human transaldolase gene (TALDO1) is located on chromosome 11 at p15.4-p15.5". Genomics 45 (1): 233–8. doi:10.1006/geno.1997.4932. PMID 9339383.

[pmid11283793-5] Verhoeven NM, Huck JH, Roos B, Struys EA, Salomons GS, Douwes AC, van der Knaap MS, Jakobs C (May 2001). "Transaldolase deficiency: liver cirrhosis associated with a new inborn error in the pentose phosphate pathway". Am. J. Hum. Genet. 68 (5): 1086–92. doi:10.1086/320108. PMC 1226089. PMID 11283793.

[pmid17613166-6] Perl A (June 2007). "The pathogenesis of transaldolase deficiency". IUBMB Life 59 (6): 365–73. doi:10.1080/15216540701387188. PMID 17613166.

[pmid15286385-7] Niland B, Perl A (2004). "Evaluation of autoimmunity to transaldolase in multiple sclerosis". Methods Mol. Med. 102: 155–71. doi:10.1385/1-59259-805-6:155. PMID 15286385.

[pmid9007983-8] Jia J, Schörken U, Lindqvist Y, Sprenger GA, Schneider G (January 1997). "Crystal structure of the reduced Schiff-base intermediate complex of transaldolase B from Escherichia coli: mechanistic implications for class I aldolases". Protein Sci. 6 (1): 119–24. doi:10.1002/pro.5560060113. PMC 2143518. PMID 9007983.

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transaldolase