2.1.1.5: betaine-homocysteine S-methyltransferase

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For detailed information about betaine-homocysteine S-methyltransferase, go to the full flat file.

Reaction

Synonyms

betaine homocysteine methyltransferase, betaine homocysteine methyltransferase-1, betaine homocysteine S-methyltransferase, betaine-homocysteine methyltransferase, betaine-homocysteine S-methyltransferase, betaine-homocysteine S-methyltransferase 2, betaine-homocysteine S-methyltransferase-2, betaine-homocysteine transmethylase, betaine:homocysteine methyltransferase, betaine:homocysteine S-methyltransferase, BHMT, BHMT-1, BHMT-2, BHMT1, BHMT2, methyltransferase, betaine-homocysteine

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.1 Methyltransferases

                2.1.1.5 betaine-homocysteine S-methyltransferase

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Results	in table
28	Activating Compound
724	AA Sequence
25	Application
1	CAS Registry Number
10	Cloned(Commentary)
7	Crystallization (Commentary)
168	Disease/ Diagnostics
6	Expression
7	General Information
8	General Stability
14	IC50 Value
100	Inhibitors
4	kcat/KM [mM/s]
3	Ki Value [mM]
58	KM Value [mM]
12	Localization
11	Metals/Ions
14	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
311	Organism
1	Oxidation Stability
8	Pathway
16	PDB ID
10	pH Optimum
1	pH Stability
1	pI Value
1	Posttranslational Modification
60	Protein Variants
11	Purification (Commentary)
4	Reaction
1	Reaction Type
89	Reference
105	Source Tissue
13	Specific Activity [micromol/min/mg]
6	Storage Stability
50	Substrates and Products (Substrate)
12	Subunits
78	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
1	Temperature Stability [°C]
37	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.1.1.5 - betaine-homocysteine S-methyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

by multiple anomalous diffraction

Homo sapiens

-

673003

molecular dynamics simulations predict that K+ ions interact with residues Asp26 and/or Glu159. Crystal structure of BHMT bound to homocysteine confirms these sites of interaction and reveals further contacts between K+ ions and BHMT residues Gly27, Gln72, Gln247, and Gly298

Homo sapiens

Q93088

735230

recombinant enzyme

Homo sapiens

-

441240

-

Rattus norvegicus

-

673003

crystals with P2(1) symmetry, assymetric unit contains the whole functional tetramer showing point symmetry 222

Rattus norvegicus

O09171

659712

recombinant enzyme

Rattus norvegicus

-

441239

dominant structural feature of wild type BHMT is an (betaalpha)8 barrel. A modeled structure of truncated BHMT suggests that this protein would assume a horseshoe fold and lack methyltransferase activity

Sus scrofa

-

733936