Cloning and characterization of acetohydroxyacid synthase from Bacillus stearothermophilus.
Five genes from the ilv-leu operon from Bacillus stearothermophilus have been sequenced. Acetohydroxyacid synthase (AHAS) and its subunits were separately cloned, purified, and characterized. This thermophilic enzyme resembles AHAS III of Escherichia coli, and regulatory subunits of AHAS III complement the catalytic subunit of the AHAS of B. stearothermophilus, suggesting that AHAS III is functionally and evolutionally related to the single AHAS of gram-positive bacteria.
Porat
Iris
I
Department of Life Sciences, Ben-Gurion University of the Negev, Beer-Sheva, 84105 Israel.
Vinogradov
Michael
M
Vyazmensky
Maria
M
Lu
Chung-Dar
CD
Chipman
David M
DM
Abdelal
Ahmed T
AT
Barak
Ze'ev
Z
D000095:Acetolactate Synthase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D000595:Amino Acid Sequence; D002384:Catalysis; D003001:Cloning, Molecular; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D008969:Molecular Sequence Data; D021122:Protein Subunits; D014633:Valine / Q000494:pharmacology
D021122:Protein Subunits; D000095:Acetolactate Synthase; D014633:Valine