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Substrate Report for: N-acetylanthranilate

N-acetylanthranilate is the substrate of the of the amidase 9micc-q7wsq8 from the Hormone-sensitive_lipase_like family. It is the product of the natural substrate 1-H-3-hydroxy-4-oxoquinaldine (3-hydroxy-2-methylquinolin-4(1H)-one) of the 1-H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase (HOD) from Arthrobacter nitroguajacolicus RU61A (artsp-hod)


General
Type Natural, Benzoate
Chemical_Nomenclature 2-acetamidobenzoic acid
Canonical SMILES CC(=O)NC1=CC=CC=C1C(=O)O
InChI InChI=1S/C9H9NO3/c1-6(11)10-8-5-3-2-4-7(8)9(12)13/h2-5H,1H3,(H,10,11)(H,12,13)
InChIKey QSACCXVHEVWNMX-UHFFFAOYSA-N
Other name(s) 2-Acetamidobenzoic acid ; N-ACETYLANTHRANILIC ACID ; 2-(Acetylamino)benzoic acid ; 2-Carboxyacetanilide ; Acetylanthranilic acid ; ZZ8 ; 2-acetamidobenzoate ; Acetamidobenzoate ; P-acetaminobenzoate ; 2-(acetylamino)benzoate ; AC1NUSR8
________________________________________________________________________________________________
MW|179.17
Formula|C9H9NO3
CAS_number|89-52-1
PubChem|6971
UniChem|QSACCXVHEVWNMX-UHFFFAOYSA-N
IUPHAR|
Wikipedia|

Target
Families | N-acetylanthranilate ligand of proteins in family: Hormone-sensitive_lipase_like, HOD-cofactorfree-dioxygenase
Stucture | 2 structures: 8OXT, 2WJ6
Protein | 9micc-q7wsq8, artsp-hod

References:
Search PubMed for references concerning: N-acetylanthranilate

1 more
    Title: Structural basis for cofactor-independent dioxygenation of N-heteroaromatic compounds at the alpha/beta-hydrolase fold
    Steiner RA, Janssen HJ, Roversi P, Oakley AJ, Fetzner S
    Ref: Proc Natl Acad Sci U S A, 107:657, 2010 : PubMed

            

    Title: N-acetylanthranilate amidase from Arthrobacter nitroguajacolicus Ru61a, an alpha/beta-hydrolase-fold protein active towards aryl-acylamides and -esters, and properties of its cysteine-deficient variant
    Kolkenbrock S, Parschat K, Beermann B, Hinz HJ, Fetzner S
    Ref: Journal of Bacteriology, 188:8430, 2006 : PubMed

            

    Title: 2,4-dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1
    Bauer I, Max N, Fetzner S, Lingens F
    Ref: European Journal of Biochemistry, 240:576, 1996 : PubMed