4.1.1.47: tartronate-semialdehyde synthase

This is an abbreviated version!
For detailed information about tartronate-semialdehyde synthase, go to the full flat file.

Reaction

2 glyoxylate =

Synonyms

GCL, Glyoxalate carboligase, Glyoxylate carbo-ligase, Glyoxylate carboligase, Glyoxylate carboxy-lyase, Glyoxylate carboxy-lyase (dimerizing and reducing), Glyoxylic carbo-ligase, Hydroxymalonic semialdehyde carboxylase, Synthase, tartronate semialdehyde, Tartronate semialdehyde carboxylase, tartronate semialdehyde synthase, Tartronate-semialdehyde synthase, Tartronic semialdehyde carboxylase, Tartronic semialdehyde synthase

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.1 Carboxy-lyases

                4.1.1.47 tartronate-semialdehyde synthase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
3379	AA Sequence
1	CAS Registry Number
3	Cloned(Commentary)
11	Cofactor
1	Crystallization (Commentary)
2	Expression
2	General Information
11	kcat/KM [mM/s]
6	KM Value [mM]
1	Localization
2	Metals/Ions
4	Molecular Weight [Da]
13	Natural Substrates/ Products (Substrates)
63	Organism
5	Pathway
6	PDB ID
1	pH Optimum
12	Protein Variants
4	Purification (Commentary)
1	Reaction
2	Reaction Type
21	Reference
11	Specific Activity [micromol/min/mg]
27	Substrates and Products (Substrate)
4	Subunits
28	Synonyms
1	Systematic Name
5	Turnover Number [1/s]

Specific Activity

print visible entries

print all entries

Specific Activity on EC 4.1.1.47 - tartronate-semialdehyde synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to Specific Activity Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

SPECIFIC ACTIVITY [µmol/min/mg]

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

0.06

Escherichia coli

-

mutant enzyme L478A, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C

727003

0.2

2 entries

0.68

Escherichia coli

-

mutant enzyme I393A, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C

727003

0.84

Escherichia coli

-

mutant enzyme I479V, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C

727003

0.93

Escherichia coli

-

mutant enzyme I393V, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C

727003

17.1

Escherichia coli K-12

P0AEP7

mutant V51S is nearly as active as the wild-type enzyme

705846

17.5

2 entries

18.3

Escherichia coli K-12

P0AEP7

mutant E52Q

705846

2.7

Escherichia coli K-12

P0AEP7

mutant V51E is about seven times slower than the wild-type enzyme

705846

0.2

Escherichia coli

-

mutant enzyme V51D, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C

727003

0.2

Escherichia coli K-12

P0AEP7

mutant V51D catalyzes the formation of the product nearly two orders of magnitude more slowly than the wild-type enzyme

705846

17.5

Escherichia coli

-

wild type enzyme, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C

727003

17.5

Escherichia coli K-12

P0AEP7

wild-type enzyme

705846