EC Number   |
General Information |
Reference |
|---|
  3.5.99.8 | evolution |
the enzyme is a metalloprotease family member |
757730 |
| 3.5.99.8 | metabolism |
Bradyrhizobium species strain JS329 metabolizes 5-nitroanthranilic acid (5NAA), a metabolite secreted by Streptomyces scabies, the bacterium responsible for potato scab, an agricultural disease of global economic importance. The first biodegradation enzyme is 5NAA-aminohydrolase (5NAA-A), a metalloprotease family member that converts 5NAA to 5-nitrosalicylic acid |
757730 |
| 3.5.99.8 | metabolism |
the enzyme catalyzes the initial step in 5-nitroanthranilic acid degradation, a hydrolytic deamination to form 5-nitrosalicylic acid, followed by ring fission catalyzed by 5NSA dioxygenase, biodegradation mechanism and pathway overview |
719725 |
| 3.5.99.8 | more |
NaaA is a hydrolytic metalloenzyme with a narrow substrate spectrum |
719725 |
| 3.5.99.8 | more |
the enzyme employs a nucleophilic aromatic substitution mechanism. 5-Nitroanthranilate aminohydrolase performs a unique deamination reaction whereby the amino group, which is para to the nitro substituent, is hydrolyzed to form 5-nitrosalicylic acid, and the nitro group remains intact. 5NAA binds primarily within one catalytic lobe but is stabilized by a key residue, Tyr223 from an adjacent monomer, which provides parallel-displaced Pi-Pi stacking stabilization. Within the catalytic lobe, 5NAA is held in place by Arg373 and Arg289, which stabilize the carboxyl and nitro groups, respectively, and the side chain of Glu158, which is within hydrogen bonding distance of the amino substituent. Asp160 and the main chain of Trp372 also stabilize the aforementioned adjacent Tyr223. Two loops disordered in the apo structure are located in this region of the catalytic lobe. Substrate binding organizes these loops, primarily by interactions between Tyr288 and Arg98 and between Asp95 and Lys286 |
757730 |
