Reference to 2.5.1.108; Id = 723158 - BRENDA Enzyme Database

-

Pyrococcus horikoshii

-

Pyrococcus horikoshii

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

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 [4Fe4S] cluster. In the reduced state, the [4Fe4S] cluster can provide one electron to reductively cleave the bound S-adenosyl-L-methionine molecule

Pyrococcus horikoshii

34000

-

2 * 34000, SDS-PAGE

Pyrococcus horikoshii

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]

-

?

Pyrococcus horikoshii

O58832

-

Pyrococcus horikoshii

wild-type and mutant enzymes

Pyrococcus horikoshii

S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2]

-

723158

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

723158

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

723158

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

723158

Pyrococcus horikoshii

S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]

-

?

homodimer

-

Pyrococcus horikoshii

homodimer

2 * 34000, SDS-PAGE

Pyrococcus horikoshii

PhDph2

-

Pyrococcus horikoshii

S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase

-

Pyrococcus horikoshii

65

-

assay at

Pyrococcus horikoshii

7.4

-

assay at

Pyrococcus horikoshii

-

Pyrococcus horikoshii

-

Pyrococcus horikoshii

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

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 [4Fe4S] cluster. In the reduced state, the [4Fe4S] cluster can provide one electron to reductively cleave the bound S-adenosyl-L-methionine molecule

Pyrococcus horikoshii

34000

-

2 * 34000, SDS-PAGE

Pyrococcus horikoshii

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]

-

?

-

Pyrococcus horikoshii

wild-type and mutant enzymes

Pyrococcus horikoshii

S-adenosyl-L-methionine + L-histidine-[translation elongation factor 2]

-

723158

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

723158

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

723158

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

723158

Pyrococcus horikoshii

S-methyl-5'-thioadenosine + 2-[(3S)-3-amino-3-carboxypropyl]-L-histidine600-[translation elongation factor 2]

-

?

homodimer

-

Pyrococcus horikoshii

homodimer

2 * 34000, SDS-PAGE

Pyrococcus horikoshii

65

-

assay at

Pyrococcus horikoshii

7.4

-

assay at

Pyrococcus horikoshii

physiological function

first step of diphthamide biosynthesis, a unique posttranslational modification on a histidine residue of translational elongation factor 2

Pyrococcus horikoshii

physiological function

first step of diphthamide biosynthesis, a unique posttranslational modification on a histidine residue of translational elongation factor 2

Pyrococcus horikoshii

758825

Fenwick

The crystal structure of Dph2 ...

Methanobrevibacter smithii, Methanobrevibacter smithii DSM 861

Biochemistry

58

4343-4351

2019

-

1

-

2

-

2

-

1

-

2

1

2

-

1

-

1

-

2

-

1

-

2

1

-

759511

Dong

The asymmetric function of Dp ...

Saccharomyces cerevisiae

J. Biol. Inorg. Chem.

24

777-782

2019

-

4

-

1

-

5

-

2

1

-

1

-

1

-

4

-

1

-

2

1

-

759725

Dong

Methods for studying the radi ...

Saccharomyces cerevisiae, Pyrococcus horikoshii, Saccharomyces cerevisiae BY4741

Methods Enzymol.

606

421-438

2018

-

2

-

3

-

72

-

2

-

3

2

3

-

2

-

2

-

3

-

2

-

3

2

-

759402

Dong

Substrate-dependent cleavage ...

Pyrococcus horikoshii

J. Am. Chem. Soc.

139

5680-5683

2017

-

3

-

1

-

3

1

-

1

-

1

-

3

-

3

1

-

738461

Dong

An organometallic complex form ...

Pyrococcus horikoshii

J. Am. Chem. Soc.

138

9755-9758

2016

-

2

-

2

-

1

-

1

-

1

-

2

-

739730

Abdel-Fattah

Insights into diphthamide, key ...

Saccharomyces cerevisiae

Toxins

5

958-968

2013

-

1

-

1

-

1

-

1

-

1

-

723158

Zhu

Mechanistic understanding of P ...

Pyrococcus horikoshii

Mol. Biosyst.

7

74-81

2011

-

1

8

-

2

1

2

-

4

-

2

-

4

2

1

-

1

-

1

-

1

8

-

2

1

2

-

2

-

4

2

1

-

1

-

1

-

723263

Zhang

Lin, H.: Diphthamide biosynthe ...

Pyrococcus horikoshii

Nature

465

891-896

2010

-

2

-

2

-

2

-

1

-

1

-

3

1

-

2

-

2

-

2

-

2

-

1

-

3

1

-

1

-

725594

Webb

Diphthamide modification of eE ...

Mus musculus

J. Cell Sci.

121

3140-3145

2008

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

1

-

718109

Liu

Identification of the proteins ...

Saccharomyces cerevisiae, Mus musculus

Mol. Cell. Biol.

24

9487-9497

2004

-

2

-

2

-

1

-

2

-

2

-

2

-

2

-

4

-

725093

Mattheakis

Diphthamide synthesis in Sacch ...

Saccharomyces cerevisiae, Saccharomyces cerevisiae FY251

Gene

132

149-154

1993

-

1

-

2

-

2

-

2

-

1

-

1

-

2

-

2

-

Mechanistic understanding of Pyrococcus horikoshii Dph2, a [4Fe-4S] enzyme required for diphthamide biosynthesis

Data extracted from this reference: