3.5.4.28: S-adenosylhomocysteine deaminase

This is an abbreviated version!
For detailed information about S-adenosylhomocysteine deaminase, go to the full flat file.

Reaction

Synonyms

deaminase, adenosylhomocysteine, MJ1541

ECTree

     3 Hydrolases

         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds

             3.5.4 In cyclic amidines

                3.5.4.28 S-adenosylhomocysteine deaminase

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Results	in table
1	Activating Compound
7694	AA Sequence
1	CAS Registry Number
1	Cloned(Commentary)
2	General Information
1	General Stability
4	Inhibitors
4	kcat/KM [mM/s]
5	KM Value [mM]
4	Metals/Ions
4	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
3	Organism
2	PDB ID
1	pH Optimum
1	pH Range
5	Protein Variants
2	Purification (Commentary)
1	Reaction
1	Reaction Type
3	Reference
1	Specific Activity [micromol/min/mg]
4	Substrates and Products (Substrate)
3	Subunits
3	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
4	Temperature Stability [°C]
5	Turnover Number [1/s]

Metals Ions

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Metals Ions on EC 3.5.4.28 - S-adenosylhomocysteine deaminase

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Fe2+

Methanocaldococcus jannaschii

Q58936

the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal

727779

Ni2+

Methanocaldococcus jannaschii

Q58936

the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal

727779

Zn2+

Methanocaldococcus jannaschii

Q58936

the activity found in the enzymes expressed with added Zn(II) and added Fe(II) are 2fold higher than when expressed with Ni(II) or without additional metal

727779

additional information

Methanocaldococcus jannaschii

Q58936

metal-dependent enzyme. The metal can not be removed from the enzyme nor can the nature of the catalytic metal be established. Dialysis of the wild-type enzyme for 3 days against a dipicolinic acid containing buffer fails to show any lowering enzyme activity, again indicating that chelation is not able to remove the bound metal in the active site. The catalytic metal is not removed by EDTA

727779