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Literature summary extracted from

  • Yao, J.; Dodson, V.J.; Frank, M.W.; Rock, C.O.
    Chlamydia trachomatis scavenges host fatty acids for phospholipid synthesis via an acyl-acyl carrier protein synthetase (2015), J. Biol. Chem., 290, 22163-22173 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.2.1.20 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

EC Number Localization Comment Organism GeneOntology No. Textmining
6.2.1.20 membrane AasC is a peripheral membrane protein Chlamydia trachomatis 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.2.1.20 Mg2+ required Chlamydia trachomatis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.20 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]
-
 ?
6.2.1.20 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]
-
 ?
6.2.1.20 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]
-
 ?
6.2.1.20 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 ?
-
 ?
6.2.1.20 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 ?
-
 ?
6.2.1.20 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

EC Number Organism UniProt Comment Textmining
6.2.1.20 Chlamydia trachomatis
-
 propagated in HeLa cells
-
6.2.1.20 Chlamydia trachomatis O84781 propagated in human cells
-
6.2.1.20 Chlamydia trachomatis 434/Bu
-
 propagated in HeLa cells
-
6.2.1.20 Chlamydia trachomatis D/UW-3/Cx O84781 propagated in human cells
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.20 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.20 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]
-
 ?
6.2.1.20 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]
-
 ?
6.2.1.20 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]
-
 ?
6.2.1.20 ATP + oleate + an [acyl-carrier protein]
-
 Chlamydia trachomatis AMP + diphosphate + oleoyl-[acyl-carrier protein]
-
 ?
6.2.1.20 ATP + oleate + an [acyl-carrier protein]
-
 Chlamydia trachomatis D/UW-3/Cx AMP + diphosphate + oleoyl-[acyl-carrier protein]
-
 ?
6.2.1.20 ATP + oleate + an [acyl-carrier protein]
-
 Chlamydia trachomatis 434/Bu AMP + diphosphate + oleoyl-[acyl-carrier protein]
-
 ?
6.2.1.20 ATP + palmitate + an [acyl-carrier protein] preferred acyl substrate Chlamydia trachomatis AMP + diphosphate + palmitoyl-[acyl-carrier protein]
-
 ?
6.2.1.20 ATP + palmitate + an [acyl-carrier protein] preferred acyl substrate Chlamydia trachomatis D/UW-3/Cx AMP + diphosphate + palmitoyl-[acyl-carrier protein]
-
 ?
6.2.1.20 ATP + palmitate + an [acyl-carrier protein] preferred acyl substrate Chlamydia trachomatis 434/Bu AMP + diphosphate + palmitoyl-[acyl-carrier protein]
-
 ?
6.2.1.20 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 ?
-
 ?
6.2.1.20 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 ?
-
 ?
6.2.1.20 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

EC Number Synonyms Comment Organism
6.2.1.20 AasC
-
 Chlamydia trachomatis
6.2.1.20 Acyl-ACP synthetase
-
 Chlamydia trachomatis
6.2.1.20 Acyl-acyl carrier protein synthetase
-
 Chlamydia trachomatis
6.2.1.20 CT776
-
 Chlamydia trachomatis
6.2.1.20 CTO_0846 gene name, UniProt Chlamydia trachomatis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.2.1.20 37
-
 assay at Chlamydia trachomatis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2.1.20 8
-
 assay at Chlamydia trachomatis

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.20 ATP
-
 Chlamydia trachomatis

General Information

EC Number General Information Comment Organism
6.2.1.20 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
6.2.1.20 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