Cloned (Comment) | Organism |
---|---|
gene aasC, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Rosetta, complementation of Escherichia coli strain LCH66 (aas-1 pldA1 pldB12) | Chlamydia trachomatis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | AasC is a peripheral membrane protein | Chlamydia trachomatis | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Chlamydia trachomatis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + a long-chain fatty acid + an [acyl-carrier protein] | Chlamydia trachomatis | the enzyme uses host cell fatty acids as substrates | AMP + diphosphate + a long-chain acyl-[acyl-carrier protein] | - |
? | |
ATP + a long-chain fatty acid + an [acyl-carrier protein] | Chlamydia trachomatis D/UW-3/Cx | the enzyme uses host cell fatty acids as substrates | AMP + diphosphate + a long-chain acyl-[acyl-carrier protein] | - |
? | |
ATP + a long-chain fatty acid + an [acyl-carrier protein] | Chlamydia trachomatis 434/Bu | the enzyme uses host cell fatty acids as substrates | AMP + diphosphate + a long-chain acyl-[acyl-carrier protein] | - |
? | |
additional information | Chlamydia trachomatis | exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo | ? | - |
? | |
additional information | Chlamydia trachomatis D/UW-3/Cx | exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo | ? | - |
? | |
additional information | Chlamydia trachomatis 434/Bu | exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Chlamydia trachomatis | - |
propagated in HeLa cells | - |
Chlamydia trachomatis | O84781 | propagated in human cells | - |
Chlamydia trachomatis 434/Bu | - |
propagated in HeLa cells | - |
Chlamydia trachomatis D/UW-3/Cx | O84781 | propagated in human cells | - |
Purification (Comment) | Organism |
---|---|
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) Rosetta to over 90% purity, purified AasC catalyzed the ATP-dependent ligation of free fatty acids to ACP | Chlamydia trachomatis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + a long-chain fatty acid + an [acyl-carrier protein] | the enzyme uses host cell fatty acids as substrates | Chlamydia trachomatis | AMP + diphosphate + a long-chain acyl-[acyl-carrier protein] | - |
? | |
ATP + a long-chain fatty acid + an [acyl-carrier protein] | the enzyme uses host cell fatty acids as substrates | Chlamydia trachomatis D/UW-3/Cx | AMP + diphosphate + a long-chain acyl-[acyl-carrier protein] | - |
? | |
ATP + a long-chain fatty acid + an [acyl-carrier protein] | the enzyme uses host cell fatty acids as substrates | Chlamydia trachomatis 434/Bu | AMP + diphosphate + a long-chain acyl-[acyl-carrier protein] | - |
? | |
ATP + oleate + an [acyl-carrier protein] | - |
Chlamydia trachomatis | AMP + diphosphate + oleoyl-[acyl-carrier protein] | - |
? | |
ATP + oleate + an [acyl-carrier protein] | - |
Chlamydia trachomatis D/UW-3/Cx | AMP + diphosphate + oleoyl-[acyl-carrier protein] | - |
? | |
ATP + oleate + an [acyl-carrier protein] | - |
Chlamydia trachomatis 434/Bu | AMP + diphosphate + oleoyl-[acyl-carrier protein] | - |
? | |
ATP + palmitate + an [acyl-carrier protein] | preferred acyl substrate | Chlamydia trachomatis | AMP + diphosphate + palmitoyl-[acyl-carrier protein] | - |
? | |
ATP + palmitate + an [acyl-carrier protein] | preferred acyl substrate | Chlamydia trachomatis D/UW-3/Cx | AMP + diphosphate + palmitoyl-[acyl-carrier protein] | - |
? | |
ATP + palmitate + an [acyl-carrier protein] | preferred acyl substrate | Chlamydia trachomatis 434/Bu | AMP + diphosphate + palmitoyl-[acyl-carrier protein] | - |
? | |
additional information | exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo | Chlamydia trachomatis | ? | - |
? | |
additional information | exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo | Chlamydia trachomatis D/UW-3/Cx | ? | - |
? | |
additional information | exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo | Chlamydia trachomatis 434/Bu | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AasC | - |
Chlamydia trachomatis |
Acyl-ACP synthetase | - |
Chlamydia trachomatis |
Acyl-acyl carrier protein synthetase | - |
Chlamydia trachomatis |
CT776 | - |
Chlamydia trachomatis |
CTO_0846 | gene name, UniProt | Chlamydia trachomatis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Chlamydia trachomatis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | Chlamydia trachomatis |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Chlamydia trachomatis |
General Information | Comment | Organism |
---|---|---|
evolution | Chlamydia trachomatis encodes for a homologue (CT776, aasC) to the C-terminal acyl-ACP synthetase domain of the bifunctional Escherichia coli Aas. The Escherichia coli aas gene encodes a bifunctional protein with 2-acyl-GPE acyltransferase activity localized in the N-terminal domain and an acyl-ACP synthetase activity in the C-terminal domain. Chlamydia trachomatis encodes adjacent genes that are homologous to the two aas domains. The CT775 gene product is related to the N-terminal Escherichia coli Aas acyltransferase domain (residues 11-149) and contains the acyltransferase catalytic HX4D motif. The CT776 gene product is related to the C-terminal acyl-ACP synthetase domain (residues 256-709) and contains the domain, which corresponds to the binding site for the acyl-adenylate intermediate | Chlamydia trachomatis |
physiological function | the CT776 gene encodes an acyl-ACP synthetase (AasC) with a substrate preference for palmitic compared with oleic acid in vitro. Exogenous fatty acids are elongated and incorporated into phospholipids by Escherichia coli-expressing AasC, illustrating its function as an acyl-ACP synthetase in vivo. Possible existence of an AasC-dependent pathway in Chlamydia trachomatis that selectively scavenges host saturated fatty acids to be used for the de novo synthesis of its membrane constituents | Chlamydia trachomatis |