Regulation of acetohydroxy acid synthase in Corynebacterium glutamicum during fermentation of α-ketobutyrate to l-isoleucine
10.1007/bf00252545 · doi-reference
Physiological implications of the substrate specificities of acetohydroxy acid synthases from varied organisms
10.1128/jb.172.6.3444-3449.1990 · doi-reference
Expression, purification and characterization of Arabidopsis thaliana acetohydroxyacid synthase
10.1042/bj3270161 · doi-reference
Binding and activation of thiamin diphosphate in acetohydroxyacid synthase
10.1021/bi0104524 · doi-reference
Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria
10.1128/jb.169.8.3750-3756.1987 · doi-reference
Application of metabolic engineering for the biotechnological production of L-valine
10.1007/s00253-014-5782-8 · doi-reference
The Corynebacterium glutamicum genome: features and impacts on biotechnological processes
10.1007/s00253-003-1328-1 · doi-reference
10.1007/978-3-642-29857-8_4
10.1007/978-3-642-29857-8_4 · doi-reference
Sixty years of thiamin diphosphate biochemistry
10.1016/s0167-4838(98)00067-3 · doi-reference
A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase
10.1016/0969-2126(93)90025-c · doi-reference
Biosynthesis of 2-aceto-2-hydroxy acids: acetolactate synthases and acetohydroxyacid synthases
10.1016/s0167-4838(98)00083-1 · doi-reference
A common structural motif in thiamin pyrophosphate-binding enzymes
10.1016/0014-5793(89)81064-6 · doi-reference
FAD-independent and herbicide-resistant mutants of tobacco acetohydroxy acid synthase
10.5012/bkcs.2005.26.6.916 · doi-reference
Electron transfer in acetohydroxy acid synthase as a side reaction of catalysis. Implications for the reactivity and partitioning of the carbanion/enamine form of (alpha-hydroxyethyl)thiamin diphosphate in a "nonredox" flavoenzyme
10.1021/bi049897t · doi-reference
Cloning and phylogenetic analysis of the genes encoding acetohydroxyacid synthase from the archaeon Methanococcus aeolicus
10.1016/s0378-1119(96)00779-2 · doi-reference
Influence of temperature on the production of an archaeal thermoactive alcohol dehydrogenase from Pyrococcus furiosus with recombinant Escherichia coli
10.1007/s00792-005-0490-z · doi-reference
Role of a conserved arginine in the mechanism of acetohydroxyacid synthase
10.1074/jbc.m401667200 · doi-reference
Acetohydroxyacid synthase isozyme I from Escherichia coli has unique catalytic and regulatory properties
10.1016/j.bbagen.2005.10.008 · doi-reference
Effect of carbon and nitrogen sources on growth dynamics and exopolysaccharide production for the hyperthermophilic archaeonThermococcus litoralis and bacterium Thermotoga maritima
10.1002/1097-0290(20000905)69:5<537::aid-bit8>3.0.co;2-7 · doi-reference
Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species
10.1111/j.1574-6976.2006.00039.x · doi-reference
Heat treatment purification of thermostable cellulase and hemicellulase enzymes expressed in E. coli
10.1016/0141-0229(89)90069-0 · doi-reference
Thermotoga lettingae sp. nov., a novel thermophilic, methanol-degrading bacterium isolated from a thermophilic anaerobic reactor
10.1099/00207713-52-4-1361 · doi-reference
Optimization of expression and properties of the recombinant acetohydroxyacid synthase of Thermotoga maritima
10.1016/j.dib.2015.09.018 · doi-reference
A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
10.1016/0003-2697(76)90527-3 · doi-reference
The bifunctional pyruvate decarboxylase/pyruvate ferredoxin oxidoreductase from Thermococcus guaymasensis
10.1155/2014/349379 · doi-reference
A colorimetric determination of blood acetoin
10.1016/s0021-9258(17)41484-0 · doi-reference
Assay of acetohydroxyacid synthase
10.1016/0003-2697(88)90139-x · doi-reference
Crystal structures of TM0549 and NE1324—two orthologs of E. coli AHAS isozyme III small regulatory subunit
10.1110/ps.072793807 · doi-reference
