2.6.1.18: beta-alanine-pyruvate transaminase

This is an abbreviated version!
For detailed information about beta-alanine-pyruvate transaminase, go to the full flat file.

Reaction

Synonyms

3FCR_4M mutant, alanine:glyoxylate aminotransferase/beta-alanine:pyruvate aminotransferase, aminotransferase, beta-alanine-pyruvate, AptA, At3g08860, ATA117 11Rd mutant, beta-A:P TAm, beta-alanine-alpha-alanine transaminase, beta-alanine-pyruvate aminotransferase, beta-alanine-pyruvate aminotransferase 3, beta-alanine:pyruvate aminotransferase, beta-alanine:pyruvate transaminase, FG99_15380, More, omega-amino acid:pyruvate transaminase, omega-TA, omega-transaminase, omega-VpTA, PAO2, S-selective omega-TA, Sthe_0848

ECTree

     2 Transferases

         2.6 Transferring nitrogenous groups

             2.6.1 Transaminases

                2.6.1.18 beta-alanine-pyruvate transaminase

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Results	in table
1	Activating Compound
2981	AA Sequence
13	Application
1	CAS Registry Number
13	Cloned(Commentary)
12	Cofactor
3	Crystallization (Commentary)
2	Expression
11	General Information
1	General Stability
12	Inhibitors
7	KM Value [mM]
2	Localization
4	Molecular Weight [Da]
10	Natural Substrates/ Products (Substrates)
2	Organic Solvent Stability
34	Organism
8	Pathway
61	PDB ID
13	pH Optimum
2	pH Range
1	pH Stability
12	Protein Variants
10	Purification (Commentary)
3	Reaction
1	Reaction Type
32	Reference
13	Source Tissue
6	Specific Activity [micromol/min/mg]
1	Storage Stability
130	Substrates and Products (Substrate)
5	Subunits
44	Synonyms
1	Systematic Name
12	Temperature Optimum [°C]
10	Temperature Stability [°C]

Engineering

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Engineering on EC 2.6.1.18 - beta-alanine-pyruvate transaminase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

R414K

2 entries

D392K

Variovorax paradoxus

-

site-directed mutagenesis, slightly reduced activity compared to wild-type enzyme

759057

E345F

Variovorax paradoxus

-

site-directed mutagenesis, reduced activity compared to wild-type enzyme

759057

E391K

Variovorax paradoxus

-

site-directed mutagenesis, reduced activity compared to wild-type enzyme

759057

G165M

2 entries

G98M

Variovorax paradoxus

-

site-directed mutagenesis, slightly reduced activity compared to wild-type enzyme

759057

G98M/D392K

Variovorax paradoxus

-

site-directed mutagenesis, reduced activity compared to wild-type enzyme

759057

G98M/E345F

Variovorax paradoxus

-

site-directed mutagenesis, reduced activity compared to wild-type enzyme

759057

additional information

2 entries

R414K

Pseudomonas sp.

-

19.9% of wild-type activity with substrate beta-alanine, 9.6% with substrate cadaverine, 20.5% with substrate 1,3-diaminopropane

737507

R414K

Pseudomonas sp. AAC

-

19.9% of wild-type activity with substrate beta-alanine, 9.6% with substrate cadaverine, 20.5% with substrate 1,3-diaminopropane

-

G165M

Variovorax paradoxus

-

best DELTADELTAG prediction, the mutant shows a 3.3fold reduction in enzymatic activity and an only a slight improvement in the Tm value, which stresses the importance of experimental evaluation of the theoretical data

759057

G165M

Variovorax paradoxus

-

site-directed mutagenesis, reduced activity compared to wild-type enzyme

759057

additional information

uncultured bacterium

-

development of beta-phenylalanine ester synthesis method from stable beta-keto ester substrate using engineered omega-transaminase. The omega-transaminase mutants 3FCR_4M and ATA117 11Rd show great potential for further engineering experiments aiming at the synthesis of chiral (S)- and (R)-phenylalanine esters. This alternative approach results in the conversion of 32% and 13% for the (S)- and (R)-enantiomer, respectively. Furthermore, the (S)-phenylalanine ethyl ester is isolated by performing a semi-preparative synthesis

759802

additional information

Variovorax paradoxus

-

synthesis and optical resolution of beta-phenylalanine and other important aromatic beta-amino acids by biotransformation utilizing an omega-transaminase (omega-TA) from Variovorax paradoxus. Design of mutant variants of the omega-TA to gain higher process stability on the basis of predictions calculated by using the FoldX software. Thermostabilization of a nonthermostable S-selective omega-TA by FoldX-guided site-directed mutagenesis. The melting point (Tm) of the best-performing mutant is increased to 59.3°C, an increase of 4.0°C relative to the Tm value of the wild-type enzyme, whereby the mutant fully retains its specific activity

759057