1.1.1.103: L-threonine 3-dehydrogenase
This is an abbreviated version!
For detailed information about L-threonine 3-dehydrogenase, go to the full flat file.
Reaction
Synonyms
CLOST_1621, L-ThrDH, L-threonine dehydrogenase, More, orf382, TDG, TDH, Thr dehydrogenase, ThrDH, threonine 3-dehydrogenase, threonine dehydrogenase
ECTree
1.1.1.103 L-threonine 3-dehydrogenaseAdvanced search results
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Engineering on EC 1.1.1.103 - L-threonine 3-dehydrogenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G184A
-
the catalytic efficiency of the mutant is 330fold lower than that of the wild type enzyme
L80G
-
the catalytic efficiency of the mutant is 3300fold lower than that of the wild type enzyme
T186N
-
the catalytic efficiency of the mutant is 330fold lower than that of the wild type enzyme
C38S
R180K
the mutation has little effect on NAD+ binding affinity, whereas affects the substrate's affinity for the enzyme
E152A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E152C
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E152D
site-directed mutagenesis, the E152D mutant shows 3-fold higher turnover rate and reduced affinities toward L-threonine and NAD+ compared to wild-type TDH, Glu152 to Asp substitution causes the enhancement of deprotonation of His47 or ionization of zinc-bound water and threonine in the enzyme-NAD+ complex
E152Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E152S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E152T
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E199A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R204A
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
D179A
mutation affects switching between the open and closed form of the enzyme. Catalytic efficiency (kcat/Km) of the mutant enzyme for L-Thr is 36fold lower than wild-type value
D179N
mutation affects switching between the open and closed form of the enzyme. Catalytic efficiency (kcat/Km) of the mutant enzyme for L-Thr is 190fold lower than wild-type value
S111A
mutation affects dehydrogenation of L-Thr directly. Catalytic efficiency (kcat/Km) of the mutant enzyme for L-Thr is 950fold lower than wild-type value
S74A
mutation affects switching between the open and closed form of the enzyme. Catalytic efficiency (kcat/Km) of the mutant enzyme for L-Thr is 317fold lower than wild-type value
T177A
mutation affects dehydrogenation of L-Thr directly. Catalytic efficiency (kcat/Km) of the mutant enzyme for L-Thr is 633fold lower than wild-type value
Y136F
mutation affects dehydrogenation of L-Thr directly. Catalytic efficiency (kcat/Km) of the mutant enzyme for L-Thr is 127fold lower than wild-type value
additional information
C38S
-
site-directed mutagenesis, catalytically inactive mutant, C38 is located in an activating divalent metal-ion binding site
C38S
-
1 cysteine residue per subunit is essential for catalytic activity and Mn2+ binding
additional information
-
all individuals examined contain at least two mutations that on translation would generate truncated proteins that would be non-functional since they have lost the splicing acceptor site preceding exon 6 and codon Arg214 is mutated to a stop codon. Therefore the gene is an expressed pseudogene
additional information
-
ste11 gene knocked out with a double crossover via homologous recombination. Monosaccharide composition of exopolysaccharide produced by the mutant strain is altered from that of ebosin. Bioactivity of the mutant is lower than ebosin
