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Literature summary extracted from

  • Shi, D.; Yu, X.; Zhao, G.; Ho, J.; Lu, S.; Allewell, N.M.; Tuchman, M.
    Crystal structure and biochemical properties of putrescine carbamoyltransferase from Enterococcus faecalis: assembly, active site, and allosteric regulation (2012), Proteins, 80, 1436-1447.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.3.6 gene agcB, expression as His-tagged protein in Escherichia coli strain BL21(DE3) Enterococcus faecalis

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.3.6 purified His-tagged wild-type PTCase, from a solution containing 200 mM magnesium sulfate, 15-17% w/v PEG 3350, 100 mM Bis-tris, pH 5.5, soaking in mother liquor containing 25% v/v ethylene glycol for 1 min for cryoprotection, X-ray diffraction structure determination and analysis at 3.2 A resolution Enterococcus faecalis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.3.6 additional information
-
 additional information in contrast to other trimeric carbamoyltransferases, PTCase binds both carbamoyl phosphate and putrescine with Hill coefficients at saturating concentrations of the other substrate of 1.53 and 1.80, respectively Enterococcus faecalis
2.1.3.6 0.101
-
 Carbamoyl phosphate pH and temperature not specified in the publication Enterococcus faecalis
2.1.3.6 0.136
-
 putrescine pH and temperature not specified in the publication Enterococcus faecalis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.3.6 carbamoyl phosphate + putrescine Enterococcus faecalis
-
 phosphate + N-carbamoylputrescine
-
 ?
2.1.3.6 carbamoyl phosphate + putrescine Enterococcus faecalis ATCC 700802
-
 phosphate + N-carbamoylputrescine
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.3.6 Enterococcus faecalis Q837U7 gene agcB
-
2.1.3.6 Enterococcus faecalis ATCC 700802 Q837U7 gene agcB
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.3.6 recombinant His-tagged protein from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography, and gel filtration Enterococcus faecalis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.3.6 carbamoyl phosphate + putrescine
-
 Enterococcus faecalis phosphate + N-carbamoylputrescine
-
 ?
2.1.3.6 carbamoyl phosphate + putrescine substrate binding structures, overview Enterococcus faecalis phosphate + N-carbamoylputrescine
-
 ?
2.1.3.6 carbamoyl phosphate + putrescine
-
 Enterococcus faecalis ATCC 700802 phosphate + N-carbamoylputrescine
-
 ?
2.1.3.6 carbamoyl phosphate + putrescine substrate binding structures, overview Enterococcus faecalis ATCC 700802 phosphate + N-carbamoylputrescine
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.3.6 More structure comparison, overview Enterococcus faecalis
2.1.3.6 trimer PTCase also has a unique structural feature: a long C-terminal helix that interacts with the adjacent subunit to enhance intersubunit interactions in the molecular trimer. The C-terminal helix os essential for both formation of the functional trimer and catalytic activity, since truncated PTCase without the C-terminal helix aggregates and has only 3% of native catalytic activity Enterococcus faecalis

Synonyms

EC Number Synonyms Comment Organism
2.1.3.6 PTCase
-
 Enterococcus faecalis

General Information

EC Number General Information Comment Organism
2.1.3.6 additional information the C-terminal helix is essential for both formation of the functional trimer and catalytic activity, since truncated PTCase without the C-terminal helix aggregates and has only 3% of native catalytic activity. Active site structure, overview Enterococcus faecalis