EC number:1.1.1.103
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.1 Acting on the CH-OH group of donors |
| 1.1.1 With NAD+ or NADP+ as acceptor |
| ID: | 1.1.1.103 | ||
|---|---|---|---|
| Description: | L-threonine 3-dehydrogenase. | ||
| Alternative Name: |
TDH. | ||
| Prosite: | PDOC00058; | ||
| PDB: |
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| Cath: | 1.10.1040.10; 3.40.50.720; 3.40.640.10; 3.90.1150.10; 3.90.180.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.1.1.103 |
| BRENDA Enzyme Link: | BRENDA 1.1.1.103 |
| KEGG Enzyme Link: | KEGG1.1.1.103 |
| BioCyc Enzyme Link: | BioCyc 1.1.1.103 |
| ExPASy Enzyme Link: | ExPASy1.1.1.103 |
| EC2PDB Enzyme Link: | EC2PDB 1.1.1.103 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.1.1.103 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.1.1.103 |
| IntEnz Enzyme Link: | IntEnz 1.1.1.103 |
| MEDLINE Enzyme Link: | MEDLINE 1.1.1.103 |
EC number:1.1.1.103
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:13161 | L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) + NADH |
| RULE(radius=1) | [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1 |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| L-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12. | Boylan SA, Dekker EE | 1981 Feb 25 | 6780553 |
| L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies. | Epperly BR, Dekker EE | 1991 Apr 5 | 2007567 |
| Highly thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis. | Bashir Q, Rashid N, Jamil F, Imanaka T, Akhtar M | 2009 Jul | 19307254 |
| Crystallization and preliminary X-ray diffraction analysis of L-threonine dehydrogenase (TDH) from the hyperthermophilic archaeon Thermococcus kodakaraensis. | Bowyer A, Mikolajek H, Wright JN, Coker A, Erskine PT, Cooper JB, Bashir Q, Rashid N, Jamil F, Akhtar M | 2008 Sep 1 | 18765916 |
| Production and characterization of a thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus. | Machielsen R, van der Oost J | 2006 Jun | 16817900 |
| Kinetic study of thermostable L-threonine dehydrogenase from an archaeon Pyrococcus horikoshii. | Higashi N, Fukada H, Ishikawa K | 2005 Feb | 16233775 |
| L-Threonine dehydrogenase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3: gene cloning and enzymatic characterization. | Shimizu Y, Sakuraba H, Kawakami R, Goda S, Kawarabayasi Y, Ohshima T | 2005 Aug | 15902509 |