Thioesterase_acyl-transferase
Relationship
Comment
This bacterial family of Acyl transferases (ACT or myristoyl-acp-specific thioesterases) catalyses the first step in the bioluminescent fatty acid reductase system, which is required for aldehyde biosynthesis. This enzyme belongs to the LuxD family. Together with acyl-protein synthetase (LuxE) and reductase (LuxC), it belongs to a multienzyme complex. This complex channels activated fatty acids into the aldehyde substrate for the luciferase-catalyzed bacterial bioluminescence reaction. The C-terminal region of LuxD interacts with LuxE to causes a conformational change. LuxD has a calculated M(r) of 34,384 and comprises 305 aa residues. Induction of luminescence only occurs at high cell density. Some bacteria have N-acylhomoserine lactone autoinducers for luminescence. Warning: the serine 77 in GXSXG motif is not the active site serine 114 as determined by X ray structure AASLS in Vibrio harveyi see Lawson et al., 2003. Family TE19 in ThYme databaseDatabase
Interpro : IPR003157 Acyl transferase, LuxD
PIRSF : PIRSF009416 lux-specific fatty acid reductase, acyl-ACP thioesterase subunit
Pdoc : No Pdoc
Pfam : PF02273 Acyl_transf_2
Prints : No Print
EC Number : No EC Number
References (5)
| Title : Thioesterase enzyme families: Functions, structures, and mechanisms - Caswell_2021_Protein.Sci__ |
| Author(s) : Caswell BT , de Carvalho CC , Nguyen H , Roy M , Nguyen T , Cantu DC |
| Ref : Protein Science , : , 2021 |
| Abstract : Caswell_2021_Protein.Sci__ |
| ESTHER : Caswell_2021_Protein.Sci__ |
| PubMedSearch : Caswell_2021_Protein.Sci__ |
| PubMedID: 34921469 |
| Title : ThYme: a database for thioester-active enzymes - Cantu_2011_Nucleic.Acids.Res_39_D342 |
| Author(s) : Cantu DC , Chen Y , Lemons ML , Reilly PJ |
| Ref : Nucleic Acids Research , 39 :D342 , 2011 |
| Abstract : Cantu_2011_Nucleic.Acids.Res_39_D342 |
| ESTHER : Cantu_2011_Nucleic.Acids.Res_39_D342 |
| PubMedSearch : Cantu_2011_Nucleic.Acids.Res_39_D342 |
| PubMedID: 21045059 |
| Title : Thioesterases: a new perspective based on their primary and tertiary structures. - Cantu_2010_Protein.Sci_19_1281 |
| Author(s) : Cantu DC , Chen Y , Reilly PJ |
| Ref : Protein Science , 19 :1281 , 2010 |
| Abstract : Cantu_2010_Protein.Sci_19_1281 |
| ESTHER : Cantu_2010_Protein.Sci_19_1281 |
| PubMedSearch : Cantu_2010_Protein.Sci_19_1281 |
| PubMedID: 20506386 |
| Title : Structure of a myristoyl-ACP-specific thioesterase from Vibrio harveyi - Lawson_1994_Biochemistry_33_9382 |
| Author(s) : Lawson DM , Derewenda U , Serre L , Ferri S , Szittner R , Wei Y , Meighen EA , Derewenda ZS |
| Ref : Biochemistry , 33 :9382 , 1994 |
| Abstract : Lawson_1994_Biochemistry_33_9382 |
| ESTHER : Lawson_1994_Biochemistry_33_9382 |
| PubMedSearch : Lawson_1994_Biochemistry_33_9382 |
| PubMedID: 8068614 |
| Gene_locus related to this paper: pholu-lxd1 , phopo-luxd , vibha-1luxd |
| Title : Sequence of the luxD gene encoding acyltransferase of the lux operon from Photobacterium leiognathi - Chao_1993_Gene_126_155 |
| Author(s) : Chao YF , Weng SF , Lin JW |
| Ref : Gene , 126 :155 , 1993 |
| Abstract : Chao_1993_Gene_126_155 |
| ESTHER : Chao_1993_Gene_126_155 |
| PubMedSearch : Chao_1993_Gene_126_155 |
| PubMedID: 8472957 |
| Gene_locus related to this paper: phole-lxd2 |
Structures (1)
Genes Proteins in Thioesterase_acyl-transferase family (17)
No fragment of genes
Structures in Thioesterase_acyl-transferase family (1)Substrates in Thioesterase_acyl-transferase family (1)
No Inhibitor