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Literature summary extracted from

  • Bera, A.; Atanasova, V.; Dhanda, A.; Ladner, J.; Parsons, J.
    Structure of aminodeoxychorismate synthase from Stenotrophomonas maltophilia (2012), Biochemistry, 51, 10208-10217 .
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.123 2.25 A crystal structure of PabB that features the 273PIAGT277 motif engaged in several interactions that hold the enzyme in a distorted conformation in the absence of substrate Stenotrophomonas maltophilia

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.123 0.24
-
chorismate pH 8, 25°C Stenotrophomonas maltophilia

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.6.1.123 Mg2+ one magnesium ion identified in the PabB structure, located outside of the active site Stenotrophomonas maltophilia

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.123 (2S)-2-amino-4-deoxychorismate + NH3 Stenotrophomonas maltophilia
-
4-amino-4-deoxychorismate + NH3
-
?
2.6.1.123 (2S)-2-amino-4-deoxychorismate + NH3 Stenotrophomonas maltophilia K279a
-
4-amino-4-deoxychorismate + NH3
-
?
2.6.1.123 2 L-glutamine + 2 H2O Stenotrophomonas maltophilia
-
2 L-glutamate + 2 NH3
-
?
2.6.1.123 2 L-glutamine + 2 H2O Stenotrophomonas maltophilia K279a
-
2 L-glutamate + 2 NH3
-
?
2.6.1.123 chorismate + 2 L-glutamine + H2O Stenotrophomonas maltophilia
-
4-amino-4-deoxychorismate + 2 L-glutamate + ammonia
-
?
2.6.1.123 chorismate + 2 L-glutamine + H2O Stenotrophomonas maltophilia K279a
-
4-amino-4-deoxychorismate + 2 L-glutamate + ammonia
-
?
2.6.1.123 chorismate + NH3 Stenotrophomonas maltophilia
-
(2S)-2-amino-4-deoxychorismate + H2O
-
?
2.6.1.123 chorismate + NH3 Stenotrophomonas maltophilia K279a
-
(2S)-2-amino-4-deoxychorismate + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.123 Stenotrophomonas maltophilia B2FR92 subunit PabB
-
2.6.1.123 Stenotrophomonas maltophilia K279a B2FR92 subunit PabB
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.123 (2S)-2-amino-4-deoxychorismate + NH3
-
Stenotrophomonas maltophilia 4-amino-4-deoxychorismate + NH3
-
?
2.6.1.123 (2S)-2-amino-4-deoxychorismate + NH3
-
Stenotrophomonas maltophilia K279a 4-amino-4-deoxychorismate + NH3
-
?
2.6.1.123 2 L-glutamine + 2 H2O
-
Stenotrophomonas maltophilia 2 L-glutamate + 2 NH3
-
?
2.6.1.123 2 L-glutamine + 2 H2O
-
Stenotrophomonas maltophilia K279a 2 L-glutamate + 2 NH3
-
?
2.6.1.123 chorismate + 2 L-glutamine + H2O
-
Stenotrophomonas maltophilia 4-amino-4-deoxychorismate + 2 L-glutamate + ammonia
-
?
2.6.1.123 chorismate + 2 L-glutamine + H2O
-
Stenotrophomonas maltophilia K279a 4-amino-4-deoxychorismate + 2 L-glutamate + ammonia
-
?
2.6.1.123 chorismate + NH3
-
Stenotrophomonas maltophilia (2S)-2-amino-4-deoxychorismate + H2O
-
?
2.6.1.123 chorismate + NH3
-
Stenotrophomonas maltophilia K279a (2S)-2-amino-4-deoxychorismate + H2O
-
?

Subunits

EC Number Subunits Comment Organism
2.6.1.123 ? x * 49500, calculated from sequence Stenotrophomonas maltophilia

Synonyms

EC Number Synonyms Comment Organism
2.6.1.123 PabB
-
Stenotrophomonas maltophilia
2.6.1.123 Smlt1032
-
Stenotrophomonas maltophilia

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.123 0.007
-
chorismate overall reaction, pH 8, 25°C Stenotrophomonas maltophilia
2.6.1.123 0.02
-
chorismate second reaction step, cosubstrate NH3, pH 8, 25°C Stenotrophomonas maltophilia

General Information

EC Number General Information Comment Organism
2.6.1.123 metabolism PabB produces 4-amino-4-deoxychorismate via a noncovalent 2-amino-2-deoxyisochorismate intermediate. 2-amino-4-deoxyisochorismate is released into solution prior to being rebound and converted to 4-amino-4-deoxyisochorismate in a second PabB-catalyzed reaction. PabB is virtually inactive alone but forms a high affinity complex with E. coli PabA Stenotrophomonas maltophilia