Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Bisht, S.; Rajaram, V.; Bharath, S.R.; Kalyani, J.N.; Khan, F.; Rao, A.N.; Savithri, H.S.; Murthy, M.R.
    Crystal structure of Escherichia coli diaminopropionate ammonia-lyase reveals mechanism of enzyme activation and catalysis (2012), J. Biol. Chem., 287, 20369-20381.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.1.15 crystal structure of DAPAL from Escherichia coli (EcDAPAL) in tetragonal and monoclinic forms at 2.0 and 2.2 A resolutions is shown Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.3.1.15 D120N mutant shows no reaction with D-DAP, Km (L-DAP) increased compared to wild-type, kcat decreased Escherichia coli
4.3.1.15 D189N Km (D-DAP) and (L-DAP) increased compared to wild-type, kcat decreased Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.1.15 0.03
-
L-2,3-diaminopropanoate wild-type, pH and temperature not specified in the publication Escherichia coli
4.3.1.15 0.05
-
D-2,3-diaminopropanoate wild-type, pH and temperature not specified in the publication Escherichia coli
4.3.1.15 0.57
-
L-2,3-diaminopropanoate mutant D120N, pH and temperature not specified in the publication Escherichia coli
4.3.1.15 11.5
-
L-2,3-diaminopropanoate mutant D189N, pH and temperature not specified in the publication Escherichia coli
4.3.1.15 12.9
-
D-2,3-diaminopropanoate mutant D189N, pH and temperature not specified in the publication Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.1.15 43300
-
calculated from cDNA Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.15 Escherichia coli P66899
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.1.15 D-2,3-Diaminopropanoate + H2O
-
Escherichia coli Pyruvate + NH3
-
?
4.3.1.15 L-2,3-Diaminopropanoate + H2O
-
Escherichia coli Pyruvate + NH3
-
?

Subunits

EC Number Subunits Comment Organism
4.3.1.15 homodimer
-
Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.3.1.15 EcDAPAL
-
Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.1.15 0.18
-
L-2,3-diaminopropanoate mutant D189N, pH and temperature not specified in the publication Escherichia coli
4.3.1.15 0.35
-
D-2,3-diaminopropanoate mutant D189N, pH and temperature not specified in the publication Escherichia coli
4.3.1.15 3.05
-
L-2,3-diaminopropanoate mutant D120N, pH and temperature not specified in the publication Escherichia coli
4.3.1.15 24.6
-
L-2,3-diaminopropanoate wild-type, pH and temperature not specified in the publication Escherichia coli
4.3.1.15 44.58
-
D-2,3-diaminopropanoate wild-type, pH and temperature not specified in the publication Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.1.15 7.5
-
assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.3.1.15 pyridoxal 5'-phosphate
-
Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.3.1.15 0.001
-
L-2,3-diaminopropanoate mutant D189N, pH and temperature not specified in the publication Escherichia coli
4.3.1.15 0.0266
-
D-2,3-diaminopropanoate mutant D189N, pH and temperature not specified in the publication Escherichia coli
4.3.1.15 5.35
-
L-2,3-diaminopropanoate mutant D120N, pH and temperature not specified in the publication Escherichia coli
4.3.1.15 820
-
L-2,3-diaminopropanoate wild-type, pH and temperature not specified in the publication Escherichia coli
4.3.1.15 890
-
D-2,3-diaminopropanoate wild-type, pH and temperature not specified in the publication Escherichia coli