Enzyme

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     2. Transferases
        2.2 Transferring aldehyde or ketonic groups
            2.2.1 Transketolases and transaldolases
ID:2.2.1.1
Description:Transketolase.
Alternative Name: Glycoaldehyde transferase.
Prosite: PDOC00635;
PDB:
PDBScop
1ITZ 8030099; 8030101; 8030102; 8042478; 8042480; 8042481; 8030099; 8030101; 8030102; 8042478; 8042480; 8042481; 8030099; 8030101; 8030102; 8042478; 8042480; 8042481;
5HHT 8024301; 8024303; 8024304; 8036680; 8036682; 8036683; 8024301; 8024303; 8024304; 8036680; 8036682; 8036683;
2R8P 8024301; 8024303; 8024304; 8036680; 8036682; 8036683; 8024301; 8024303; 8024304; 8036680; 8036682; 8036683;
2R8O 8024301; 8024303; 8024304; 8036680; 8036682; 8036683; 8024301; 8024303; 8024304; 8036680; 8036682; 8036683;
1QGD 8024301; 8024303; 8024304; 8036680; 8036682; 8036683; 8024301; 8024303; 8024304; 8036680; 8036682; 8036683;
 » show all

Cath: 3.40.50.920; 3.40.50.970;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.2.1.1
BRENDA Enzyme Link: BRENDA 2.2.1.1
KEGG Enzyme Link: KEGG2.2.1.1
BioCyc Enzyme Link: BioCyc 2.2.1.1
ExPASy Enzyme Link: ExPASy2.2.1.1
EC2PDB Enzyme Link: EC2PDB 2.2.1.1
ExplorEnz Enzyme Link: ExplorEnz 2.2.1.1
PRIAM enzyme-specific profiles Link: PRIAM 2.2.1.1
IntEnz Enzyme Link: IntEnz 2.2.1.1
MEDLINE Enzyme Link: MEDLINE 2.2.1.1
MSA:

2.2.1.1;

Phylogenetic Tree:

2.2.1.1;

Uniprot:
M-CSA:
RHEA:27626 D-erythrose 4-phosphate + D-xylulose 5-phosphate = beta-D-fructose 6-phosphate + D-glyceraldehyde 3-phosphate
RULE(radius=1) [*:1]-[CH2;+0:2]-[C;H0;+0:3](=[O;H0;+0:4])-[*:5]-[*:6]-[OH;+0:7].[*:8]-[CH;+0:9](-[OH;+0:10])-[CH;+0:11]=[O;H0;+0:12]>>[*:1]-[C;H0;+0:2]1(-[CH2;+0:11]-[OH;+0:12])-[O;H0;+0:7]-[*:6]-[*:5]-[CH;+0:3]-1-[OH;+0:4].[*:8]-[CH;+0:9]=[O;H0;+0:10]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

RHEA:10508 D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
RULE(radius=1) [*:1]-[CH;+0:2]=[O;H0;+0:3].[*:4]=[C;H0;+0:5](-[CH2;+0:6]-[*:7])-[CH;+0:8](-[*:9])-[CH;+0:10](-[*:11])-[OH;+0:12]>>[*:9]-[CH2;+0:8]-[C;H0;+0:10](-[*:11])=[O;H0;+0:12].[*:4]=[CH;+0:5]-[CH;+0:6](-[*:7])-[CH;+0:2](-[*:1])-[OH;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Properties and functions of the thiamin diphosphate dependent enzyme transketolase.Schenk G, Duggleby RG, Nixon PF1998 Dec9924800
Identification of catalytically important residues in yeast transketolase.Wikner C, Nilsson U, Meshalkina L, Udekwu C, Lindqvist Y, Schneider G1997 Dec 169398292
Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis.Nilsson U, Meshalkina L, Lindqvist Y, Schneider G1997 Jan 178999873
Molecular characterization of transketolase (EC 2.2.1.1) active in the Calvin cycle of spinach chloroplasts.Flechner A, Dressen U, Westhoff P, Henze K, Schnarrenberger C, Martin W1996 Nov8980496
His103 in yeast transketolase is required for substrate recognition and catalysis.Wikner C, Meshalkina L, Nilsson U, Bäckström S, Lindqvist Y, Schneider G1995 Nov 18521838
Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes. Crystal structures of yeast transketolase in complex with analogs of thiamin diphosphate.König S, Schellenberger A, Neef H, Schneider G1994 Apr 88144674
Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains.Sprenger GA, Schörken U, Sprenger G, Sahm H1995 Jun 17607225
Mutations in TKT Are the Cause of a Syndrome Including Short Stature, Developmental Delay, and Congenital Heart Defects.Boyle L, Wamelink MMC, Salomons GS, Roos B, Pop A, Dauber A, Hwa V, Andrew M, Douglas J, Feingold M, Kramer N, Saitta S, Retterer K, Cho MT, Begtrup A, Monaghan KG, Wynn J, Chung WK2016 Jun 227259054
Structure and function of the transketolase from Mycobacterium tuberculosis and comparison with the human enzyme.Fullam E, Pojer F, Bergfors T, Jones TA, Cole ST2012 Jan22645655
Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate.Asztalos P, Parthier C, Golbik R, Kleinschmidt M, Hübner G, Weiss MS, Friedemann R, Wille G, Tittmann K2007 Oct 3017914867
Effects of transketolase cofactors on its conformation and stability.Esakova OA, Meshalkina LE, Kochetov GA2005 Nov 1916125202
Mutations in the transketolase-like gene TKTL1: clinical implications for neurodegenerative diseases, diabetes and cancer.Coy JF, Dressler D, Wilde J, Schubert P200515991799
Structure and properties of an engineered transketolase from maize.Gerhardt S, Echt S, Busch M, Freigang J, Auerbach G, Bader G, Martin WF, Bacher A, Huber R, Fischer M2003 Aug12913150