2.5.1.49: O-acetylhomoserine aminocarboxypropyltransferase

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For detailed information about O-acetylhomoserine aminocarboxypropyltransferase, go to the full flat file.

Reaction

Synonyms

AHS, EC 4.2.99.10, gamma-cyano-alpha-aminobutyric acid synthase, Homocysteine synthase, MetC, methionine synthase, MetY, O-acetyl-L-homoserine (thiol)-lyase, O-acetyl-L-homoserine acetate-lyase (adding methanethiol), O-acetyl-L-homoserine sulfhydrolase, o-acetyl-L-homoserine sulfhydrylase, O-acetylhomoserine sulfhydrolase, O-acetylhomoserine sulfhydrylase, OAH, OAH SHase, OAH SHLase, OAH sulfhydrylase, OAH-OAS sulfhydrylase, oah2 gene product, OAHS, OAS-OAH sulfhydrylase, Q187D4

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)

                2.5.1.49 O-acetylhomoserine aminocarboxypropyltransferase

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Results	in table
5	Activating Compound
11400	AA Sequence
3	Application
1	CAS Registry Number
9	Cloned(Commentary)
15	Cofactor
2	Crystallization (Commentary)
2	Disease/ Diagnostics
1	General Information
6	General Stability
2	IC50 Value
74	Inhibitors
3	kcat/KM [mM/s]
17	Ki Value [mM]
41	KM Value [mM]
2	Metals/Ions
32	Molecular Weight [Da]
25	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
47	Organism
7	Pathway
16	PDB ID
13	pH Optimum
4	pH Range
4	pH Stability
1	pI Value
18	Purification (Commentary)
1	Reaction
4	Reaction Type
43	Reference
16	Source Tissue
38	Specific Activity [micromol/min/mg]
6	Storage Stability
145	Substrates and Products (Substrate)
23	Subunits
51	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]
1	Temperature Range [°C]
6	Temperature Stability [°C]
3	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.5.1.49 - O-acetylhomoserine aminocarboxypropyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

to 2.1 A resolution, space group P21

Mycobacterium tuberculosis

L7N4M1

721214

to 2.2 A resolution, space group C2, two monomers per asymmetric unit. The monomer adopts an alpha/beta fold and consists of a large central seven-stranded beta-sheet, a two-stranded beta-sheet and a three-stranded beta-sheet. The beta-sheets are flanked by a total of 12 alpha-helices and two 3(10)-helices. The active site is located near the N-terminus of alpha3. The pydridoxal 5'-phosphate-binding site is occupied by water molecules in the absence of the cofactor. The phosphate group of pydridoxal 5'-phosphate makes hydrogen bonds to Thr204, Ser202 and the amide N-atoms of Gly83 and Met84. Asp180 is within salt-bridge distance of the N1 atom of pydridoxal 5'-phosphate. Leu353, Met183, Ile87 and Met84 interact with the hydrophobic region of pydridoxal 5'-phosphate

Wolinella succinogenes

Q7M844

721161