2.1.3.9: N-acetylornithine carbamoyltransferase

This is an abbreviated version!
For detailed information about N-acetylornithine carbamoyltransferase, go to the full flat file.

Reaction

Synonyms

acetylornithine transcarbamylase, AOTC, AOTCase, MJ0366, More, N-acetyl-L-ornithine transcarbamylase, N-acetylornithine carbamoyltransferase, N-acetylornithine transcarbamoylase, N-acetylornithine transcarbamylase

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.3 Carboxy- and carbamoyltransferases

                2.1.3.9 N-acetylornithine carbamoyltransferase

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Results	in table
978	AA Sequence
1	CAS Registry Number
2	Cloned(Commentary)
3	Crystallization (Commentary)
5	General Information
5	Natural Substrates/ Products (Substrates)
7	Organism
5	Pathway
15	PDB ID
1	Posttranslational Modification
4	Protein Variants
1	Purification (Commentary)
2	Reaction
1	Reaction Type
7	Reference
6	Substrates and Products (Substrate)
17	Synonyms
1	Systematic Name

General Information

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General Information on EC 2.1.3.9 - N-acetylornithine carbamoyltransferase

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

evolution

Xanthomonas campestris

Q8P8J2

AOTCase is involved in an arginine biosynthesis pathway in plant pathogens of the Xanthomonadaceae family such as Xylella and Xanthomonas

718880

metabolism

Xanthomonas campestris

Q8P8J2

AOTCase is involved in an arginine biosynthesis pathway in plant pathogens of the Xanthomonadaceae family such as Xylella and Xanthomonas

718880

physiological function

Xanthomonas campestris

Q8P8J2

arginine biosynthesis

706491

additional information

3 entries

additional information

Xanthomonas campestris

Q8P8J2

Lys302 is post-translationally carboxylated. The carboxyl group on Lys302 forms a strong hydrogen bonding network with surrounding active site residues, Lys252, Ser253, His293, and Glu92 from the adjacent subunit either directly or via a water molecule. The carboxyl group is involved in binding N-acetyl-L-ornithine via a water molecule. The posttranslational modification of lysine 302 has an important role in catalysis

718880

additional information

Xanthomonas campestris

-

Lys302 is post-translationally carboxylated. The carboxyl group on Lys302 forms a strong hydrogen bonding network with surrounding active site residues, Lys252, Ser253, His293, and Glu92 from the adjacent subunit either directly or via a water molecule. The carboxyl group is involved in binding N-acetyl-L-ornithine via a water molecule. The posttranslational modification of lysine 302 has an important role in catalysis

718880

additional information

Methanocaldococcus jannaschii

-

stochastic simulations of coarse-grained protein models used to investigate the propensity to form knots in early stages of protein folding, comparison of natively-knotted N-acetylornithine carbamoyltransferase, AOTCase, and an unknotted ornithine carbamoyltransferase, OTCase, EC 2.1.3.3, protein and amino acid interactions, mechanism, overview. The different entanglement of the two transcarbamylases follows from the tendency of the C-terminal to point away from (for OTCase) or approach and eventually thread (for AOTCase) other regions of partly-folded protein. The analysis of the OTCase/AOTCase pair clarifies that natively-knotted proteins can spontaneously knot during early folding stages and that non-native sequence-dependent interactions are important for promoting and disfavouring early knotting events. Knotting usually results from the threading of the C-terminal through loops present in the loose protein globule. Simulation of the early folding process of the two transcarbamylases, non-native interactions, kinetics, and modeling, overview

720803