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Literature summary extracted from

  • Dickert, S.; Pierik, A.J.; Buckel, W.
    Molecular characterization of phenyllactate dehydratase and its initiator from Clostridium sporogenes (2002), Mol. Microbiol., 44, 49-60 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
5.6.1.9 expression in Escherichia coli Clostridium sporogenes

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.6.1.9 Iron FldI contains 4.1 non-heme iron and 2.3 acid-labile sulfur atoms per homodimer Clostridium sporogenes

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.175 Clostridium sporogenes Q93AL9 and Q93AL8 Q93AL9 i.e. alpha-subunit FldB, Q93AL8 i.e. beta-subunit FldC
-
5.6.1.9 Clostridium sporogenes Q93AM0
-
-

Oxidation Stability

EC Number Oxidation Stability Organism
5.6.1.9 FldI is extremely sensitive towards exposure to oxygen, which results in denaturation and precipitation of the protein. The half-life under air is less than 1 min. Clostridium sporogenes

Purification (Commentary)

EC Number Purification (Comment) Organism
5.6.1.9 recombinant preotein. During all procedures, FldI was stabilized with 1 mM ATP and 5 mM MgCl2 under an atmosphere of 95% N2 and 5% H2 Clostridium sporogenes

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.175 (R)-3-(4-hydroxyphenyl)lactoyl-CoA
-
 Clostridium sporogenes (E)-4-coumaroyl-CoA + H2O
-
 ?
4.2.1.175 (R)-3-(indol-3-yl)lactoyl-CoA
-
 Clostridium sporogenes 3-(indol-3-yl)acryloyl-CoA + H2O
-
 ?
4.2.1.175 (R)-3-(phenyl)lactoyl-CoA
-
 Clostridium sporogenes (E)-cinnamoyl-CoA + H2O
-
 ?
5.6.1.9 2 ATP + a reduced flavodoxin + inactive phenyllactate dehydratase + 2 H2O
-
 Clostridium sporogenes 2 ADP + 2 phosphate + a flavodoxin semiquinone + active phenyllactate dehydratase
-
 ?

Subunits

EC Number Subunits Comment Organism
4.2.1.175 ? x * 46239, subunit FldB, and x * 43150, subunit FldC, calculated from sequence. X * 45490, subunit FldB, and x * 37420, subunit FldC, MALDI-TOF Clostridium sporogenes
5.6.1.9 ? x * 28077, calculated from sequence, x * 28000-29000, SDS-PAGE Clostridium sporogenes

Synonyms

EC Number Synonyms Comment Organism
4.2.1.175 (R)-phenyllactyl-CoA dehydratase
-
 Clostridium sporogenes
4.2.1.175 FldB
-
 Clostridium sporogenes
4.2.1.175 FldC
-
 Clostridium sporogenes
5.6.1.9 fldI
-
 Clostridium sporogenes

Cofactor

EC Number Cofactor Comment Organism Structure
5.6.1.9 4Fe-4S-center FldI contains one [4Fe-4S]1+/2+ cluster with an electron spin S = 3/2 in the reduced form Clostridium sporogenes

pI Value

EC Number Organism Comment pI Value Maximum pI Value
4.2.1.175 Clostridium sporogenes subunit FldB, calculated from sequence
-
 5.9
5.6.1.9 Clostridium sporogenes calculated from sequence
-
 8

General Information

EC Number General Information Comment Organism
4.2.1.175 physiological function heterotrimeric phenyllactate dehydratase, FldABC, catalyses the reversible dehydration of (R)-phenyllactate to (E)-cinnamate in two steps: first CoA-transfer from the cofactor cinnamoyl-CoA to phenyllactate to yield phenyllactyl-CoA and the product cinnamate mediated by FldA, a (R)-phenyllactate CoA-transferase, second dehydration of phenyllactyl-CoA to cinnamoyl-CoA mediated by heterodimeric FldBC, a phenyllactyl-CoA dehydratase. Phenyllactate dehydratase requires initiation by ATP, MgCl2 and a reducing agent such as dithionite mediated by an extremely oxygen-sensitive initiator protein (FldI) present in the cell-free extract Clostridium sporogenes
5.6.1.9 physiological function FldI is an oxygen-sensitive initiator protein required for initial activation of phenyllactate dehydratase, EC 4.2.1.175. In the oxidized state, FldI exhibits significant ATPase activity, which appears to be essential for unidirectional electron transfer Clostridium sporogenes