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Literature summary for 2.3.1.178 extracted from

  • Richter, A.A.; Kobus, S.; Czech, L.; Hoeppner, A.; Zarzycki, J.; Erb, T.J.; Lauterbach, L.; Dickschat, J.S.; Bremer, E.; Smits, S.H.J.
    The architecture of the diaminobutyrate acetyltransferase active site provides mechanistic insight into the biosynthesis of the chemical chaperone ectoine (2020), J. Biol. Chem., 295, 2822-2838 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
heterologous production of EctA in Escherichia coli, with either a N-terminal (NH2-WSHPQFEK-SG) or a C-terminal (SA-WSHPQFEK-COOH) Strep-Tag II peptide for their purification by affinity chromatography Paenibacillus lautus

Crystallization (Commentary)

Crystallization (Comment) Organism
high-resolution crystal structures at 1.2-2.2 A resolution: 1. for its apo-form, 2. in complex with CoA, 3. in complex with L-2,4-diaminobutanoate, 4. in complex with both CoA and L-2,4-diaminobutanoate, and 5. in the presence of the product (2S)-4-acetamido-2-aminobutanoate Paenibacillus lautus

Inhibitors

Inhibitors Comment Organism Structure
NaCl 100 mM, 25% loss of activity. 1.5 M, 88% loss of activity Paenibacillus lautus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.13
-
L-2,4-diaminobutanoate pH 7.4, 30°C Paenibacillus lautus
2.79
-
acetyl-CoA pH 7.5, 30°C Paenibacillus lautus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39730
-
gel filtration Paenibacillus lautus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + L-2,4-diaminobutanoate Paenibacillus lautus the enzyme catalyzes a step in ectoine biosynthesis CoA + (2S)-4-acetamido-2-aminobutanoate
-
?

Organism

Organism UniProt Comment Textmining
Paenibacillus lautus A0A385TZ63
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Paenibacillus lautus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + L-2,4-diaminobutanoate
-
Paenibacillus lautus CoA + (2S)-4-acetamido-2-aminobutanoate
-
?
acetyl-CoA + L-2,4-diaminobutanoate the enzyme catalyzes a step in ectoine biosynthesis Paenibacillus lautus CoA + (2S)-4-acetamido-2-aminobutanoate
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 20120, enzyme withe a C-terminal (SA-WSHPQFEK-COOH) Strep-Tag II peptide, SDS-PAGE Paenibacillus lautus
homodimer 2 * 20550, enzyme with a N-terminal (NH2-WSHPQFEK-SG) Strep-Tag II peptide, SDS-PAGE Paenibacillus lautus

Synonyms

Synonyms Comment Organism
EctA
-
Paenibacillus lautus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
the enzyme is only active for very short times at temperatures higher than 40 °C Paenibacillus lautus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5 9.5
-
Paenibacillus lautus

General Information

General Information Comment Organism
evolution crystal structures of the enzyme in complex with the cosubstrate reveals an evolutionarily conserved CoA-binding site Paenibacillus lautus
metabolism the enzyme catalyzes a step in ectoine biosynthesis Paenibacillus lautus