2.3.1.35: glutamate N-acetyltransferase

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For detailed information about glutamate N-acetyltransferase, go to the full flat file.

Reaction

Synonyms

acetylglutamate synthetase, acetylglutamate-acetylornithine transacetylase, acetylglutamic synthetase, acetylglutamic-acetylornithine transacetylase, acetylornithinase, acetylornithine glutamate acetyltransferase, acetyltransferase, glutamate, alpha-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase, argJ, CcOATase, CLGAT, glutamate acetyltransferase, glutamate N-acetyltransferase, L-ornithine acetyltransferase, Mtb OAT, N-acetyl-L-glutamate synthetase, OAT, OAT2, OATase, ornithine acetyl transferase, ornithine acetyltransferase, ornithine transacetylase

ECTree

     2 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.35 glutamate N-acetyltransferase

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Results	in table
1	Activating Compound
28972	AA Sequence
3	Application
1	CAS Registry Number
15	Cloned(Commentary)
1	Cofactor
6	Crystallization (Commentary)
40	General Information
4	General Stability
3	IC50 Value
22	Inhibitors
3	Ki Value [mM]
22	KM Value [mM]
3	Localization
15	Molecular Weight [Da]
37	Natural Substrates/ Products (Substrates)
58	Organism
3	Oxidation Stability
5	Pathway
40	PDB ID
13	pH Optimum
3	pH Range
14	Posttranslational Modification
26	Protein Variants
8	Purification (Commentary)
3	Reaction
1	Reaction Type
46	Reference
2	Source Tissue
29	Specific Activity [micromol/min/mg]
3	Storage Stability
60	Substrates and Products (Substrate)
15	Subunits
73	Synonyms
1	Systematic Name
10	Temperature Optimum [°C]
2	Temperature Range [°C]
2	Temperature Stability [°C]

Reaction

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Reaction on EC 2.3.1.35 - glutamate N-acetyltransferase

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate

3 entries

N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate

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N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate

substrate binding structure, oxyanion stabilization mechanism of the enzyme-substrate complex, the ping pong reaction mechanism involves Gly112 and Thr181, active site structure

Streptomyces clavuligerus

P0DJQ5

660991

N2-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L-glutamate

residue T181 becomes acetylated and the carbonyl oxygen of the acyl-enzyme complex is located in an oxyanion hole and positioned to hydrogen bond with the backbone amide-NH of G112 and the alcohol of T111. Presence of two distinct acyl-enzyme complex structures which can interconvert by movement of the T111 side-chain alcohol hydrogen away from the oxyanion hole to hydrogen bond with the backbone carbonyl of the acylated residue, T181

Streptomyces clavuligerus

P0DJQ5

704194