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

BRENDA support

Literature summary for 2.3.1.94 extracted from

  • Charkoudian, L.K.; Liu, C.W.; Capone, S.; Kapur, S.; Cane, D.E.; Togni, A.; Seebach, D.; Khosla, C.
    Probing the interactions of an acyl carrier protein domain from the 6-deoxyerythronolide B synthase (2011), Protein Sci., 20, 1244-1255.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.94

Protein Variants

Protein Variants Comment Organism
additional information site-directed mutagenesis to identify ACP residues that contribute to the observed specificity. Module 3 of the 6-deoxyerythronolide B synthase is reengineered to catalyze two successive rounds of chain elongation Saccharopolyspora erythraea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Saccharopolyspora erythraea unidirectional translocation of the growing polyketide chain along the 6-deoxyerythronolide B synthase, ratchet mechanism, overview ?
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharopolyspora erythraea
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information unidirectional translocation of the growing polyketide chain along the 6-deoxyerythronolide B synthase, ratchet mechanism, overview Saccharopolyspora erythraea ?
-
 ?

Subunits

Subunits Comment Organism
More solution structure of ACP2, the tertiary fold of ACP2 is a three-helix bundle, overview Saccharopolyspora erythraea

Synonyms

Synonyms Comment Organism
6-deoxyerythronolide B synthase
-
 Saccharopolyspora erythraea

General Information

General Information Comment Organism
additional information enzyme-substrate interactions are involved in the translocation of a polyketide from ACP2 to ketosynthase KS3, the ACP domain of the 6-deoxyerythronolide B synthase contributes to its association with its ketosynthase, KS, translocation partner, models for KS-ACP recognition during chain elongation and chain translocation, docking model, overview. Determination of selective protein–protein interactions between the two partners using CF3-S-ACP as probe. The acyl chain substrate also has a significant influence on this interaction Saccharopolyspora erythraea