2-Methyl-L-tryptophan is a substrate of tryptophanase.
Tryptophanase was generally considered to be inactive towards tryptophan derivatives substituted at 2-position of the indole ring. We have shown that cells containing tryptophanase catalyze the formation of 2-methyl-L-tryptophan from 2-methylindole and L-serine, and from 2-methylindole, pyruvate and ammonium ion. The kinetics of pyruvate formation from 2-methyl-L-tryptophan and its alpha-deuterated analogue catalyzed by homogeneous tryptophanase were examined. The primary deuterium isotope effect (kH/kD = 4.0) as well as the absorption spectrum of tryptophanase complex with 2-methyl-L-tryptophan indicate that the rate of enzymatic reaction of 2-methyl-L-tryptophan is in a considerable degree determined by the stage of removal of alpha-proton.
Faleev
N G
NG
Institute of Food Substances, Russian Academy of Sciences, Moscow.
Gogoleva
O I
OI
Dementieva
I S
IS
Zakomirdina
L N
LN
Belikov
V M
VM
D000042:Absorption; D003903:Deuterium / Q000737:chemistry; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism; D007211:Indoles / Q000378:metabolism; D007477:Ions; D007700:Kinetics; D011773:Pyruvates / Q000737:chemistry / Q000378:metabolism; D019289:Pyruvic Acid; D000644:Quaternary Ammonium Compounds / Q000737:chemistry / Q000378:metabolism; D012694:Serine / Q000378:metabolism; D013379:Substrate Specificity; D014364:Tryptophan / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism*; D014368:Tryptophanase / Q000378:metabolism* / Q000493:pharmacokinetics
D007211:Indoles; D007477:Ions; D011773:Pyruvates; D000644:Quaternary Ammonium Compounds; C095863:2-methyltryptophan; D012694:Serine; D019289:Pyruvic Acid; D014364:Tryptophan; D003903:Deuterium; D014368:Tryptophanase; C022958:2-methylindole