| Name | AHAS |
|---|---|
| Synonyms | 209L8; AHAS; Acetolactate synthase; Acetolactate synthase homolog; ILV2H; ILVB like; ILVBL; IlvB (Bacterial acetolactate synthase) like isoform 1 variant… |
| Name | sulfometuron |
|---|---|
| CAS | 2-[[[[(4,6-dimethyl-2-pyrimidinyl)amino]carbonyl]amino]sulfonyl]benzoic acid |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 15709745 | McCourt JA, Pang SS, Guddat LW, Duggleby RG: Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase. Biochemistry. 2005 Feb 22;44(7):2330-8. Here we report crystal structures of yeast AHAS in complex with chlorsulfuron (at a resolution of 2.19 A), sulfometuron methyl (2.34 A), and two other sulfonylureas, metsulfuron methyl (2.29 A) and tribenuron methyl (2.58 A). |
84(1,1,1,4) | Details |
| 12011332 | Lapidot M, Raveh D, Sivan A, Arad SM, Shapira M: Stable chloroplast transformation of the unicellular red alga Porphyridium species. Plant Physiol. 2002 May;129(1):7-12. AHAS is the target enzyme of the herbicide sulfometuron methyl, which effectively inhibits growth of bacteria, fungi, plants, and algae. |
84(1,1,1,4) | Details |
| 8576056 | Epelbaum S, Chipman DM, Barak Z: Metabolic effects of inhibitors of two enzymes of the branched-chain amino acid pathway in Salmonella typhimurium. J Bacteriol. 1996 Feb;178(4):1187-96. One inhibitor was the sulfonylurea herbicide sulfometuron methyl (SMM), which inhibits this isozyme and AHAS of other organisms, and the other was N-isopropyl oxalylhydroxamate (IpOHA), which inhibits ketol-acid reductoisomerase (KARI). |
83(1,1,1,3) | Details |
| 18337064 | Sohn H, Lee KS, Ko YK, Ryu JW, Woo JC, Koo DW, Shin SJ, Ahn SJ, Shin AR, Song CH, Jo EK, Park JK, Kim HJ: In vitro and ex vivo activity of new derivatives of acetohydroxyacid synthase inhibitors against Mycobacterium tuberculosis and non-tuberculous mycobacteria. Int J Antimicrob Agents. 2008 Jun;31(6):567-71. Epub 2008 Mar 12. Sulfometuron methyl (SM) is an inhibitor of acetohydroxyacid synthase (AHAS), the first common enzyme in the branched-chain amino acid biosynthetic pathway, and shows activity against Mycobacterium tuberculosis both in vitro and in vivo. |
82(1,1,1,2) | Details |
| 3654579 | Xing RY, Whitman WB: Sulfometuron methyl-sensitive and -resistant acetolactate synthases of the archaebacteria Methanococcus spp. J Bacteriol. 1987 Oct;169(10):4486-92. |
6(0,0,1,1) | Details |
| 17718999 | Choi KJ, Noh KM, Kim DE, Ha BH, Kim EE, Yoon MY: Identification of the catalytic subunit of acetohydroxyacid synthase in Haemophilus influenzae and its potent inhibitors. Arch Biochem Biophys. 2007 Oct 1;466(1):24-30. Epub 2007 Jul 28. Acetohydroxyacid synthase (AHAS; EC 2.2.1.6) is a - (ThDP)- and FAD-dependent enzyme that catalyzes the first common step in the biosynthetic pathway of the branched-amino acids (BCAAs) and Through which, AVS-2087 (IC (50)=0.53 microM), KSW30191 (IC (50)=1.42 microM), and KHG20612 (IC (50)=4.91 microM) displayed potent inhibition as compare to sulfometuron methyl (IC (50)=276.31 microM). |
4(0,0,0,4) | Details |
| 16667756 | Landstein D, Chipman DM, Arad SM, Barak Z: Acetohydroxy Acid Synthase Activity in Chlorella emersonii under Auto- and Heterotrophic Growth Conditions. Plant Physiol. 1990 Oct;94(2):614-620. Acetohydroxyacid synthase (AHAS) activity was studied in the green unicellular alga Chlorella emersonii. |
3(0,0,0,3) | Details |
| 1991719 | Tarleton JC, Ely B: Isolation and characterization of ilvA, ilvBN, and ilvD mutants of Caulobacter crescentus. J Bacteriol. 1991 Feb;173(3):1259-67. C. crescentus strains resistant to the herbicide sulfometuron methyl, which is known to inhibit the action of certain acetohydroxyacid synthases in a variety of bacteria and plants, were shown to contain mutations at the ilvB locus, further suggesting that an acetohydroxyacid synthase gene resides at this locus. The DNA in these plasmids hybridized to the corresponding genes of Escherichia coli and Serratia marcescens, confirming the presence of ilvB-like and ilvD-like DNA sequences at the ilvB and ilvD loci, respectively. |
1(0,0,0,1) | Details |