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Literature summary for 2.5.1.108 extracted from

  • Zhu, X.; Dzikovski, B.; Su, X.; Torelli, A.; Zhang, Y.; Ealick, S.; Freed, J.; Lin, H.
    Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis (2011), Mol. Biosyst., 7, 74-81.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.108

Cloned(Commentary)

Cloned (Comment) Organism
-
 Pyrococcus horikoshii

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Pyrococcus horikoshii

Protein Variants

Protein Variants Comment Organism
C163A difference in the EPR spectrum of the reduced form, pronounced rhombic main features with greatly increased g-value anisotropy, mutant enzyme is able to transfer the the 3-amino-3-carboxypropyl group onto His600 Pyrococcus horikoshii
C163A mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster Pyrococcus horikoshii
C259A/C287A homodimeric mutant enzyme not stable. It is inactive and cannot bind a [4Fe-4S] cluster. Heterodimeric enzyme with a wild-type subunit and a mutant subunit is active Pyrococcus horikoshii
C287A difference in the EPR spectrum, g-tensors are more axial than wild type, mutant enzyme is able to transfer the the 3-amino-3-carboxypropyl group onto His600 Pyrococcus horikoshii
C287A mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster Pyrococcus horikoshii
C59A difference in the EPR spectrum, g-tensors are more axial than wild type, mutant enzyme is able to transfer the the 3-amino-3-carboxypropyl group onto His600 Pyrococcus horikoshii
C59A mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster Pyrococcus horikoshii
C59A/C287A inactive mutant lacks the Fe-S cluster. A heterodimer of wild-type subunit and C59A/C287A mutant subunit is stable and active Pyrococcus horikoshii

Metals/Ions

Metals/Ions Comment Organism Structure
Iron-sulfur cluster each monomer contains three conserved cysteine residues that can bind a [4Fe-4S] cluster. In the reduced state, the [4Fe-4S] cluster can provide one electron to reductively cleave the bound S-adenosyl-L-methionine molecule. The chemistry requires only one [4Fe-4S] cluster to be present in the Dph2 dimer although each monomer can bind a [4Fe-4S] cluster Pyrococcus horikoshii
Iron-sulfur cluster each monomer of the dimeric enzyme contains three conserved cysteine residues that can bind a [4Fe–4S] cluster. In the reduced state, the [4Fe–4S] cluster can provide one electron to reductively cleave the bound S-adenosyl-L-methionine molecule Pyrococcus horikoshii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
 2 * 34000, SDS-PAGE Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] Pyrococcus horikoshii first step of diphthamide biosynthesis, a unique posttranslational modification on a histidine residue of translational elongation factor 2 S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2]
-
 ?
S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2] Pyrococcus horikoshii the enzyme is involved in diphthamide biosynthesis S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]
-
 ?

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O58832
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus horikoshii
wild-type and mutant enzymes Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2]
-
 Pyrococcus horikoshii S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2]
-
 ?
S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2] first step of diphthamide biosynthesis, a unique posttranslational modification on a histidine residue of translational elongation factor 2 Pyrococcus horikoshii S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine-[translation elongation factor 2]
-
 ?
S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2] the enzyme is involved in diphthamide biosynthesis Pyrococcus horikoshii S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]
-
 ?
S-adenosyl-L-methionine + L-histidine600-[translation elongation factor 2] the 3-amino-3-carboxypropyl radical is added to the imidazole ring in the pathway towards the formation of the product Pyrococcus horikoshii S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]
-
 ?

Subunits

Subunits Comment Organism
homodimer
-
 Pyrococcus horikoshii
homodimer 2 * 34000, SDS-PAGE Pyrococcus horikoshii

Synonyms

Synonyms Comment Organism
PhDph2
-
 Pyrococcus horikoshii
S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase
-
 Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
 assay at Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Pyrococcus horikoshii

General Information

General Information Comment Organism
physiological function first step of diphthamide biosynthesis, a unique posttranslational modification on a histidine residue of translational elongation factor 2 Pyrococcus horikoshii