N-acetylornithine carbamoyltransferase

Function

N-acetylornithine carbamoyltransferase (AOCT) catalyzes the reversible conversion of carbamoyl phosphate and N-acetyl-L-ornithine into N-acetyl-L-citrulline and phosphate.

Structural highlights

AOCT motif HCLP interacts with the produce acetyl citrulline. The ^[1]. Water molecules are shown as red spheres.

N-acetylornithine carbamoyltransferase complex with acetylornithine, glycerol and sulfate (PDB code 3kzn)

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3D structures of N-acetylornithine carbamoyltransferase3D structures of N-acetylornithine carbamoyltransferase

Updated on 21-July-2019

3m4j - XcAOCT + acetyl-phosphonoacetyl ornithine - Xanthomonas campestris
3m4n, 3m5c, 3m5d - XcAOCT (mutant) + acetyl-phophonoacetyl ornithine
3kzc - XcAOCT
3kzm - XcAOCT + carbamylphosphate
3kzn - XcAOCT + acetyl ornithine
3kzk - XcAOCT + acetyl citrulline
3kzo - XcAOCT + acetyl norvaline + carbamyl phosphate
3l02, 3l04, 3l05, 3l06 - XcAOCT (mutant) + norvaline derivative + carbamyl phosphate

ReferencesReferences

↑ Shi D, Yu X, Roth L, Morizono H, Tuchman M, Allewell NM. Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis. Proteins. 2006 Aug 1;64(2):532-42. PMID:16741992 doi:10.1002/prot.21013

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Joel L. Sussman, Alexander Berchansky

[1] Shi D, Yu X, Roth L, Morizono H, Tuchman M, Allewell NM. Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis. Proteins. 2006 Aug 1;64(2):532-42. PMID:16741992 doi:10.1002/prot.21013

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