2.5.1.108: 2-(3-amino-3-carboxypropyl)histidine synthase

This is an abbreviated version!
For detailed information about 2-(3-amino-3-carboxypropyl)histidine synthase, go to the full flat file.

Reaction

Synonyms

diphthamide biosynthesis protein 2, diphthine synthase, Dph1-Dph2, Dph2, DPH4, PhDph2, S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase

ECTree

     2 Transferases

         2.5 Transferring alkyl or aryl groups, other than methyl groups

             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)

                2.5.1.108 2-(3-amino-3-carboxypropyl)histidine synthase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
9173	AA Sequence
9	Cloned(Commentary)
7	Cofactor
4	Crystallization (Commentary)
8	General Information
1	Localization
4	Metals/Ions
3	Molecular Weight [Da]
17	Natural Substrates/ Products (Substrates)
85	Organism
2	Pathway
8	PDB ID
1	pH Optimum
12	Protein Variants
6	Purification (Commentary)
3	Reaction
16	Reference
1	Source Tissue
23	Substrates and Products (Substrate)
14	Subunits
21	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]

Engineering

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Engineering on EC 2.5.1.108 - 2-(3-amino-3-carboxypropyl)histidine synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to Protein Variants Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

C163A

2 entries

C259A/C287A

Pyrococcus horikoshii

O58832

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

723158

C287A

2 entries

C59A

2 entries

C59A/C287A

Pyrococcus horikoshii

O58832

inactive mutant lacks the Fe-S cluster. A heterodimer of wild-type subunit and C59A/C287A mutant subunit is stable and active

723158

C106A

Saccharomyces cerevisiae

-

the mutant shows wild type activity

759511

C128A

Saccharomyces cerevisiae

-

the mutant shows reduced activity compared to the wild type enzyme

759511

C304A

Saccharomyces cerevisiae

-

the mutant shows wild type activity

759511

C362A

Saccharomyces cerevisiae

-

the mutant shows reduced activity compared to the wild type enzyme

759511

C163A

Pyrococcus horikoshii

O58832

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

723158

C163A

Pyrococcus horikoshii

O58832

mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster

723158

C287A

Pyrococcus horikoshii

O58832

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

723158

C287A

Pyrococcus horikoshii

O58832

mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster

723158

C59A

Pyrococcus horikoshii

O58832

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

723158

C59A

Pyrococcus horikoshii

O58832

mutant enzyme has lower activity than wild-type enzyme and can bind a [4Fe-4S] cluster

723158