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Literature summary for 4.2.1.144 extracted from

  • Kim, C.G.; Yu, T.W.; Fryhle, C.B.; Handa, S.; Floss, H.G.
    3-Amino-5-hydroxybenzoic acid synthase, the terminal enzyme in the formation of the precursor of mC7N units in rifamycin and related antibiotics (1998), J. Biol. Chem., 273, 6030-6040.
    View publication on PubMed
Search for more literature for 4.2.1.144

Activating Compound

Activating Compound Comment Organism Structure
3-deoxy-D-arabinoheptulosonic acid 7-phosphate 1 mM, 40-50% activation Amycolatopsis mediterranei

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Amycolatopsis mediterranei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.164
-
 5-amino-5-deoxy-3-dehydroshikimate pH 7.5, 28°C Amycolatopsis mediterranei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39000
-
 2 * 39000, SDS-PAGE, 2 * 46101, calculated Amycolatopsis mediterranei
46101
-
 2 * 39000, SDS-PAGE, 2 * 46101, calculated Amycolatopsis mediterranei
74000
-
 gel filtration Amycolatopsis mediterranei

Organism

Organism UniProt Comment Textmining
Amycolatopsis mediterranei O52552
-
-

Purification (Commentary)

Purification (Comment) Organism
both native and recombinant protein Amycolatopsis mediterranei

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
72
-
 pH 7.5, 28°C, native enzyme Amycolatopsis mediterranei
195
-
 pH 7.5, 28°C, recombinant enzyme Amycolatopsis mediterranei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-amino-5-deoxy-3-dehydroshikimate
-
 Amycolatopsis mediterranei 3-amino-5-hydroxybenzoate + H2O
-
 ?
additional information no substrates: 5-deoxy-5-amino-3-dehydroquinic acid, 5-deoxy-5-aminoshikimic acid, quinic acid, 3-dehydroquinic acid, or 3-dehydroshikimic acid Amycolatopsis mediterranei ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 39000, SDS-PAGE, 2 * 46101, calculated Amycolatopsis mediterranei

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
33
-
-
 Amycolatopsis mediterranei

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
28 50 more than 84% of maximum activity within Amycolatopsis mediterranei

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Amycolatopsis mediterranei

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate enzyme is a dimer containing one molecule of pyridoxal phosphate per subunit. The enzyme-bound pyridoxal phosphate forms a Schiff’s base with the amino group of 5-deoxy-5-amino-3-dehydroshikimic acid and catalyzes both an alpha,beta-dehydration and a stereospecific 1,4-enolization of the substrate Amycolatopsis mediterranei