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Literature summary extracted from

  • Quadri, L.; Keating, T.; Patel, H.; Walsh, C.
    Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin In vitro reconstitution of aryl-4,2-bisthiazoline synthetase activity from PchD, PchE, and PchF (1999), Biochemistry, 38, 14941-14954 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.2.1.61 expression in Escherichia coli Pseudomonas aeruginosa
6.2.1.69 expression in Escherichia coli Pseudomonas aeruginosa

Protein Variants

EC Number Protein Variants Comment Organism
6.2.1.69 C1606A/S1607A thioesterase domain active site double mutant, fails to turn over, but a monocyclic hydroxyphenyl-thiazolinyl-cysteine product continues to be released from subunit PchE Pseudomonas aeruginosa

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.2.1.69 0.11
-
L-cysteine pH 8.8, 30°C Pseudomonas aeruginosa
6.2.1.69 0.537
-
L-cysteine pH 8.8, 30°C Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.69 (L-cysteinyl)adenylate + holo-[L-cysteinyl-carrier protein] Pseudomonas aeruginosa
-
AMP + L-cysteinyl-[L-cysteinyl-carrier protein]
-
?
6.2.1.69 ATP + L-cysteine Pseudomonas aeruginosa
-
diphosphate + (L-cysteinyl)adenylate
-
?
6.2.1.69 ATP + L-cysteine + holo-[L-cysteinyl-carrier protein] Pseudomonas aeruginosa
-
AMP + diphosphate + L-cysteinyl-[L-cysteinyl-carrier protein]
-
?
6.2.1.69 additional information Pseudomonas aeruginosa the formation of cysteinyl-S-cysteinyl-carrier protein in PchE and PchF is an acylation in-cis, in which the cysteine transferase activity of each synthetase's adenylation domain loads cysteine on the cysteinyl-carrier protein domain located within the same polypeptide. No substrate: D-cysteine ?
-
-

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.61 Pseudomonas aeruginosa Q9RFM9
-
-
6.2.1.69 Pseudomonas aeruginosa Q9RFM7 isoform PchF
-
6.2.1.69 Pseudomonas aeruginosa Q9RFM8 isoform PchE
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.2.1.69 phospholipoprotein posttranslational modification by covalent attachment of the 4'-phosphopantetheine moiety of coenzyme A is essential for the biosynthetic competence. In PchE, possible domains for phosphopantetheinylation are an N-terminal aryl carrier protein domain and a C-terminal peptidyl carrier protein domain Pseudomonas aeruginosa
6.2.1.69 phospholipoprotein posttranslational modification by covalent attachment of the 4'-phosphopantetheine moiety of coenzyme A is essential for the biosynthetic competence. PchF has a single carrier protein domain (PCP2), and is phosphopantetheinylated with a stoichiometry of 67% Pseudomonas aeruginosa

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.61 recombinant protein Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.61 (salicyl)adenylate + holo-[non-ribosomal peptide synthase PchE]
-
Pseudomonas aeruginosa AMP + salicyl-[non-ribosomal peptide synthase PchE]
-
?
6.2.1.61 ATP + salicylate
-
Pseudomonas aeruginosa diphosphate + (salicyl)adenylate
-
?
6.2.1.61 ATP + salicylate + holo-[non-ribosomal peptide synthase PchE]
-
Pseudomonas aeruginosa AMP + diphosphate + salicyl-[non-ribosomal peptide synthase PchE]
-
?
6.2.1.69 (L-cysteinyl)adenylate + holo-[L-cysteinyl-carrier protein]
-
Pseudomonas aeruginosa AMP + L-cysteinyl-[L-cysteinyl-carrier protein]
-
?
6.2.1.69 ATP + L-cysteine
-
Pseudomonas aeruginosa diphosphate + (L-cysteinyl)adenylate
-
?
6.2.1.69 ATP + L-cysteine + holo-[L-cysteinyl-carrier protein]
-
Pseudomonas aeruginosa AMP + diphosphate + L-cysteinyl-[L-cysteinyl-carrier protein]
-
?
6.2.1.69 additional information the formation of cysteinyl-S-cysteinyl-carrier protein in PchE and PchF is an acylation in-cis, in which the cysteine transferase activity of each synthetase's adenylation domain loads cysteine on the cysteinyl-carrier protein domain located within the same polypeptide. No substrate: D-cysteine Pseudomonas aeruginosa ?
-
-

Synonyms

EC Number Synonyms Comment Organism
6.2.1.61 (2,3-dihydroxybenzoyl)adenylate synthase
-
Pseudomonas aeruginosa
6.2.1.61 pchD
-
Pseudomonas aeruginosa
6.2.1.61 salicyl-AMP ligase
-
Pseudomonas aeruginosa
6.2.1.69 non-ribosomal peptide synthetase
-
Pseudomonas aeruginosa
6.2.1.69 PChE
-
Pseudomonas aeruginosa
6.2.1.69 pchF
-
Pseudomonas aeruginosa

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.2.1.69 0.63
-
L-cysteine pH 8.8, 30°C Pseudomonas aeruginosa
6.2.1.69 6.9
-
L-cysteine pH 8.8, 30°C Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
6.2.1.61 physiological function enzyme is involved in biogenesis of the nonribosomal peptide siderophore pyochelin Pseudomonas aeruginosa
6.2.1.69 physiological function protein PchD, PchE, and PchF are involved in biogenesis of the nonribosomal peptide siderophore pyochelin. PchE and PchF activate the cysteine as adenylate. PchD, PchE, and PchF produce the tricyclic acid hydroxyphenyl-thiazolyl-thiazolinyl-carboxylic acid. The three proteins contain three adenylation domains, one specific for salicylate activation and two specific for cysteine activation, and three carrier protein domains (two in PchE and one in PchF) that undergo posttranslational priming with phosphopantetheine to enable covalent tethering of salicyl and cysteinyl moieties as acyl-S-enzyme intermediates. Two cyclization domains (Cy1 in PchE and Cy2 in PchF) create the two amide linkages in the elongating chains and the cyclodehydrations of acylcysteine moieties into thiazolinyl rings. The ninth domain, the most downstream domain in PchF, is the chain-terminating, acyl-S-enzyme thioester hydrolase that releases the hydroxyphenyl-thiazolyl-thiazolinyl-carboxylic acid-S-enzyme intermediate to the tandem bis-heterocyclic acid product Pseudomonas aeruginosa

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.2.1.69 6.7
-
L-cysteine pH 8.8, 30°C Pseudomonas aeruginosa
6.2.1.69 13.3
-
L-cysteine pH 8.8, 30°C Pseudomonas aeruginosa