4.4.1.23: 2-hydroxypropyl-CoM lyase

This is an abbreviated version!
For detailed information about 2-hydroxypropyl-CoM lyase, go to the full flat file.

Reaction

Synonyms

coenzyme M-epoxyalkane ligase, Ea-CoMT, EaCoMT, EC 4.2.99.19, epoxyalkane coenzyme M transferase, epoxyalkane:2-mercaptoethanesulfonate transferase, epoxyalkane:CoM transferase, epoxyalkyl:CoM transferase, epoxypropane:coenzyme M transferase, epoxypropyl:CoM transferase, EtnE, transferase, epoxyalkyl:coenzyme M

ECTree

     4 Lyases

         4.4 Carbon-sulfur lyases

             4.4.1 Carbon-sulfur lyases (only sub-subclass identified to date)

                4.4.1.23 2-hydroxypropyl-CoM lyase

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Results	in table
321	AA Sequence
1	Application
1	CAS Registry Number
3	Cloned(Commentary)
1	Inhibitors
2	KM Value [mM]
3	Metals/Ions
1	Molecular Weight [Da]
7	Natural Substrates/ Products (Substrates)
22	Organism
4	Pathway
2	pH Optimum
1	pH Range
4	Protein Variants
2	Purification (Commentary)
2	Reaction
1	Reaction Type
17	Reference
14	Specific Activity [micromol/min/mg]
34	Substrates and Products (Substrate)
1	Subunits
20	Synonyms
1	Systematic Name
1	Temperature Optimum [°C]
1	Turnover Number [1/s]

Metals Ions

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Metals Ions on EC 4.4.1.23 - 2-hydroxypropyl-CoM lyase

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Co2+

Xanthobacter autotrophicus

-

the inactive and Zn-deficient form of enzyme is activated by addition of ZnCl2 or CoCl2

393831

Zn

Xanthobacter autotrophicus

-

Zn plays a key role in activating an organic thiol substrate for nucleophilic attack on an alkyl-donating substrate, removal of Zn results in loss of catalytic activity, the inactive and Zn-deficient form of enzyme is activated by addition of ZnCl2 or CoCl2. Thermodynamic characterization of the interaction of CoM with an enzyme-bound Zn center

393831

Zn2+

Xanthobacter autotrophicus

-

the inactive and Zn-deficient form of enzyme is activated by addition of ZnCl2 or CoCl2

393831