Reference on EC 4.1.99.1 - tryptophanase
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REF. 
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kiick, D.M.; Phillips, R.S.
Mechanistic deductions from multiple kinetic and solvent deuterium isotope effects and pH studies of pyridoxal phosphate dependent carbon-carbon lyases: Escherichia coli tryptophan indole-lyase
Biochemistry
27
7339-7344
1988
Escherichia coli
Behbahani-Nejad, I.; Dye, J.L.; Suelter, C.H.
Tryptophanase from Escherichia coli B/1t7-A
Methods Enzymol.
142
414-422
1987
Escherichia coli, Escherichia coli B/1t7-A
Honda, T.; Tokushige, M.
Effects of temperature and monovalent cations on activity and quaternary structure of tryptophanase
J. Biochem.
100
679-685
1986
Escherichia coli
Behbahani-Nejad, I.; Suelter, C.H.; Dye, J.L.
Kinetics of tryptophanase inactivation/activation by sudden removal/addition of potassium ions with the aid of a crown ether or cryptand
Curr. Top. Cell. Regul.
24
219-228
1984
Escherichia coli, Escherichia coli B/1t7-A
Whitt, D.D.; Klug, M.J.; DeMoss, R.D.
Trypotophanase from a marine bacterium, Vibrio K-7 synthesis, purification and some chemical catalytic properties
Arch. Microbiol.
122
169-175
1979
Vibrio sp., Vibrio sp. K-7
Suelter, C.H.; Snell, E.E.
Monovalent cation activation of tryptophanase
J. Biol. Chem.
252
1852-1857
1977
Escherichia coli, Escherichia coli B/1t7-A
Toraya, T.; Nihira, T.; Fukui, S.
Essential role of monovalent cations in the firm binding of pyridoxal 5'-phosphate to tryptophanase and beta-tyrosinase
Eur. J. Biochem.
69
411-419
1976
Escherichia coli, Escherichia coli B/1t7-A
-
Snell, E.E.
Tryptophanase: structure, catalytic activities, and mechanism of action
Adv. Enzymol. Relat. Areas Mol. Biol.
42
287-333
1975
Aeromonas hydrophila, Aeromonas sp., Paenibacillus alvei, Bacillus sp. (in: Bacteria), Bacteroides sp., Corynebacterium sp., Escherichia coli, Enterobacter sp., Erwinia sp., Kluyvera sp., Micrococcus sp., no activity in Acetobacter sp., no activity in Achromobacter sp., no activity in Agrobacterium sp., no activity in Alcaligenes sp., no activity in Azotobacter sp., no activity in Clostridium sp., no activity in Flavobacterium sp., no activity in Mycoplasma sp., no activity in Pseudomonas sp., no activity in Rhizobium sp., no activity in Salmonella sp., no activity in Serratia sp., no activity in Xanthomonas sp., Paracolobactrum sp., Pasteurella sp., Photobacterium sp., Providencia rettgeri, Proteus sp., Sphaerophorus sp., Vibrio sp.
Raibaud, O.; Goldberg, M.E.
The dissociated tryptophanase subunit is inactive
J. Biol. Chem.
251
2820-2824
1976
Escherichia coli
Simard, C.; Mardini, A.; Bordeleau, L.M.
Differentiation of tryptophanases of five species of Enterobacteriaceae by sulfhydryl groups
Can. J. Microbiol.
21
841-845
1975
Escherichia aurescens, Escherichia coli, Escherichia coli B / ATCC 11303, Morganella morganii, Proteus vulgaris, Shigella alkalescens
Simard, C.; Mardini, A.; Bordeleau, L.M.
The effect of pyridoxal phosphate on the tryptophanases of five species of Enterobacteriaceae
Can. J. Microbiol.
21
834-840
1975
Escherichia aurescens, Escherichia coli, Escherichia coli B / ATCC 11303, Morganella morganii, Proteus vulgaris, Shigella alkalescens
Simard, C.; Mardini, A.; Bordeleau, L.M.
Physical and chemical properties of tryptophenases of five species of Enterobacteriaceae
Can. J. Microbiol.
21
828-833
1975
Escherichia aurescens, Escherichia coli, Escherichia coli B / ATCC 11303, Morganella morganii, Proteus vulgaris, Shigella alkalescens
Yoshida, H.; Kumagai, H.; Yamada, H.; Matsubara, H.
The tryptophanase from Proteus rettgeri, improved purification and properties of crystalline holotryptophanase
Biochim. Biophys. Acta
391
494-503
1975
Providencia rettgeri
Cecchini, G.; Bojanowski, R.J.; DeMoss, R.D.
Tryptophanase from Sphaerophorus funduliformis. Purification, molecular weight and subunit properties
Biochim. Biophys. Acta
386
340-351
1975
Fusobacterium necrophorum subsp. funduliforme
Fukui, S.; Ikeda, S.; Fujimura, M.
Comparative studies on the properties of tryptophanase and tyrosine phenol-lyase immobilized directly on Sepharose or by use of Sepharose-bound pyridoxal 5 -phosphate
Eur. J. Biochem.
51
155-164
1975
Escherichia coli, Escherichia coli B/1t7-A
Yoshida, H.; Utagawa, T.; Kumagai, H.; Yamada, H.
Purification, crystallization and properties of tryptophanase from Proteus rettgeri
Agric. Biol. Chem.
38
2065-2072
1974
Providencia rettgeri
-
Yoshida, H.; Kumagai, H.; Yamada, H.
Cofactor requirement of tryptophanase from Proteus rettgeri
Agric. Biol. Chem.
38
2073-2079
1974
Providencia rettgeri
-
London, J.; Skrzynia, C.; Goldberg, M.E.
Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Evidence for the existence of nucleation centers
Eur. J. Biochem.
47
409-415
1974
Escherichia coli
Yoshida, H.; Kumagai, H.; Yamada, H.
Catalytic properties of tryptophanase from Proteus rettgeri
Agric. Biol. Chem.
38
463-464
1974
Providencia rettgeri, Providencia rettgeri AJ2770
-
Cowell, J.L.; DeMoss, R.D.
Trytophanase from Aeromonas liquefaciens. Subunit structure and aggregation of the enzyme into enzymatically active polymeric species
J. Biol. Chem.
248
6262-6269
1973
Aeromonas hydrophila
Cowell, J.L.; Moser, K.; DeMoss, R.D.
Tryptophanase from Aeromonas liquefaciens. Purification, molecular weight and some chemical, catalytic and immunochemical properties
Biochim. Biophys. Acta
315
449-463
1973
Aeromonas hydrophila, Paenibacillus alvei, Escherichia coli, Micrococcus aerogenes, Paracolobactrum coliforme, Fusobacterium necrophorum subsp. funduliforme
-
Raibaud, O.; Goldberg, M.E.
The tryptophanase from Escherichia coli K-12. II. Comparison of the thermal stabilities of apo-, holo-, and hybrid enzymes
J. Biol. Chem.
248
3451-3455
1973
Escherichia coli
O'Neill Hoch, S.; DeMoss, R.D.
Catalytic studies on tryptophanase from Bacillus alvei
J. Bacteriol.
114
341-350
1973
Paenibacillus alvei
Watanabe, T.; Snell, E.E.
Reversibility of the tryptophanase reaction: synthesis of tryptophan from indole, pyruvate, and ammonia
Proc. Natl. Acad. Sci. USA
69
1086-1090
1972
Escherichia coli
London, J.; Goldberg, M.E.
The tryptophanase from Escherichia coli K-12. I. Purification, physical properties, and quaternary structure
J. Biol. Chem.
247
1566-1570
1972
Escherichia coli
Nihira, T.; Toraya, T.; Fukui, S.
Pyridoxal-5 -phosphate-sensitized photoinactivation of tryptophanase and evidence for essential histidyl residues in the active sites
Eur. J. Biochem.
101
341-347
1979
Escherichia coli, Escherichia coli B/1t7-A
Tani, S.; Tsujimoto, N.; Kawata, Y.; Tokushige, M.
Overproduction and crystallization of tryptophanase from recombinant cells of Escherichia coli
Biotechnol. Appl. Biochem.
12
28-33
1990
Escherichia coli, Escherichia coli B/1t7-A
Taylor, H.V.; Yudkin, M.D.
Synthesis of tryptophanase in Escherichia coli: isolation and characterization of a structural-gene mutant and two regulatory mutants
Mol. Gen. Genet.
165
95-102
1978
Escherichia coli
Kawasaki, K.; Yokota, A.; Tomita, F.
Enzymatic synthesis of L-tryptophan by Enterobacter aerogenes tryptophanase highly expressed in Escherichia coli, and some properties of the purified enzyme
Biosci. Biotechnol. Biochem.
59
1938-1943
1995
Klebsiella aerogenes, Escherichia coli, Klebsiella aerogenes SM-18
Suzuki, S.; Hirahara, T.; Horinouchi, S.; Beppu, T.
Purification and properties of thermostable tryptophanase from an obligately symbiotic thermophile, Symbiobacterium thermophilum
Agric. Biol. Chem.
55
3059-3066
1991
Symbiobacterium thermophilum, Symbiobacterium thermophilum T
Faleev, N.G.; Dementieva, I.S.; Zakomirdina, L.N.; Gogoleva, O.I.; Belikov, V.M.
Tryptophanase from Escherichia coli: catalytic and spectral properties in water-organic solvents
Biochem. Mol. Biol. Int.
34
209-216
1994
Escherichia coli
Isupov, M.N.; Antson, A.A.; Dodson, E.J.; Dodson, G.G.; Dementieva, I.S.; Zakomirdina, L.N.; Wilson, K.S.; Dauter, Z.; Lebedev, A.A.; Harutyunyan, E.M.
Crystal structure of tryptophanase
J. Mol. Biol.
276
603-623
1998
Proteus vulgaris
Kawasaki, K.; Yokota, A.; Oita, S.; Kobayashi, C.; Yoshikawa, S.; Kawamoto, S.i.; Takao, S.; Tomita, F.
Cloning and characterization of a tryptophanase gene from Enterobacter aerogenes SM-18 [published erratum appears in J Gen Microbiol 1994 Apr;140(Pt 4):999
J. Gen. Microbiol.
139
3275-3281
1993
Klebsiella aerogenes, Klebsiella aerogenes SM-18
Erez, T.; Gdalevsky, G.Y.; Hariharan, C.; Pines, D.; Pines, E.; Phillips, R.S.; Cohen-Luria, R.; Parola, A.H.
Cold-induced enzyme inactivation: how does cooling lead to pyridoxal phosphate-aldimine bond cleavage in tryptophanase?
Biochim. Biophys. Acta
1594
335-340
2002
Escherichia coli
Ikushiro, H.; Kagamiyama, H.
Activation of the coenzyme at the early step of the catalytic cycle of tryptophanase
Biofactors
11
97-99
2000
Escherichia coli
Di Martino, P.; Merieau, A.; Phillips, R.; Orange, N.; Hulen, C.
Isolation of an Escherichia coil strain mutant unable to form biofilm on polystyrene and to adhere to human pneumocyte cells: involvement of tryptophanase
Can. J. Microbiol.
48
132-137
2002
Escherichia coli
Gogoleva, O.I.; Zakomirdina, L.N.; Demidkina, T.V.; Phillips, R.S.; Faleev, N.G.
Tryptophanase in aqueous methanol: the solvent effects and a probable mechanism of the hydrophobic control of substrate specificity
Enzyme Microb. Technol.
32
843-850
2003
Escherichia coli
-
Phillips, R.S.; Demidkina, T.V.; Zakomirdina, L.N.; Bruno, S.; Ronda, L.; Mozzarelli, A.
Crystals of tryptophan indole-lyase and tyrosine phenol-lyase form stable quinonoid complexes
J. Biol. Chem.
277
21592-21597
2002
Proteus vulgaris
Kudo, H.; Natsume, R.; Nishiyama, M.; Horinouchi, S.
Analysis of stability and catalytic properties of two tryptophanases from a thermophile
Protein Eng.
12
687-692
1999
Symbiobacterium thermophilum
Pioselli, B.; Bettati, S.; Demidkina, T.V.; Zakomirdina, L.N.; Phillips, R.S.; Mozzarelli, A.
Tyrosine phenol-lyase and tryptophan indole-lyase encapsulated in wet nanoporous silica gels: Selective stabilization of tertiary conformations
Protein Sci.
13
913-924
2004
Proteus vulgaris
Kogan, A.; Gdalevsky, G.Y.; Cohen-Luria, R.; Parola, A.H.; Goldgur, Y.
Crystallization and preliminary X-ray analysis of the apo form of Escherichia coli tryptophanase
Acta Crystallogr. Sect. D
60
2073-2075
2004
Escherichia coli
Phillips, R.S.; Holtermann, G.
Differential effects of temperature and hydrostatic pressure on the formation of quinonoid intermediates from L-Trp and L-Met by H463F mutant Escherichia coli tryptophan indole-lyase
Biochemistry
44
14289-14297
2005
Escherichia coli
Kulikova, V.V.; Zakomirdina, L.N.; Dementieva, I.S.; Phillips, R.S.; Gollnick, P.D.; Demidkina, T.V.; Faleev, N.G.
Tryptophanase from Proteus vulgaris: The conformational rearrangement in the active site, induced by the mutation of tyrosine 72 to phenylalanine, and its mechanistic consequences
Biochim. Biophys. Acta
1764
750-757
2006
Proteus vulgaris
Grudniak, A.M.; Nowicka-Sans, B.; Maciag, M.; Wolska, K.I.
Influence of Escherichia coli DnaK and DnaJ molecular chaperones on tryptophanase (TnaA) amount and GreA, GreB stability
FEMS Microbiol. Rev.
49
507-512
2004
Escherichia coli
Mateus, D.M.; Alves, S.S.; Da Fonseca, M.M.
Kinetics of L-tryptophan production from indole and L-serine catalyzed by whole cells with tryptophanase activity
J. Biosci. Bioeng.
97
289-293
2004
Escherichia coli, Escherichia coli B1t-7A
Ku, S.Y.; Yip, P.; Howell, P.L.
Structure of Escherichia coli tryptophanase
Acta Crystallogr. Sect. D
62
814-823
2006
Escherichia coli (P0A853), Escherichia coli, Escherichia coli JM109 (P0A853)
Swiegers, J.H.; Capone, D.L.; Pardon, K.H.; Elsey, G.M.; Sefton, M.A.; Francis, I.L.; Pretorius, I.S.
Engineering volatile thiol release in Saccharomyces cerevisiae for improved wine aroma
Yeast
24
561-574
2007
Escherichia coli
Tsesin, N.; Kogan, A.; Gdalevsky, G.Y.; Himanen, J.P.; Cohen-Luria, R.; Parola, A.H.; Goldgur, Y.; Almog, O.
The structure of apo tryptophanase from Escherichia coli reveals a wide-open conformation
Acta Crystallogr. Sect. D
D63
969-974
2007
Escherichia coli
Almog, O.; Kogan, A.; de Leeuw, M.; Gdalevsky, G.Y.; Cohen-Luria, R.; Parola, A.H.
Structural insights into cold inactivation of tryptophanase and cold adaptation degrees of subtilisin S41: Minireview
Biopolymers
89
354-359
2008
Escherichia coli (P0A853)
Gubica, T.; Boroda, E.; Temeriusz, A.; Kanska, M.
Effects of native and permethylated cyclodextrins on the catalytic activity of L-tryptophan indole lyase
J. Inclusion Phenom. Macrocyclic Chem.
54
283-288
2006
Escherichia coli
-
Chattoraj, D.K.
Tryptophanase in sRNA control of the Escherichia coli cell cycle
Mol. Microbiol.
63
1-3
2007
Escherichia coli
Kim, Y.; Lee, D.; Kim, D.; Cho, J.; Yang, J.; Chung, M.; Kim, K.; Ha, N.
Inhibition of proliferation in colon cancer cell lines and harmful enzyme activity of colon bacteria by Bifidobacterium adolescentis SPM0212
Arch. Pharm. Res.
31
468-473
2008
Rattus norvegicus
Gubica, T.; Winnicka, E.; Temeriusz, A.; Kanska, M.
The influence of selected O-alkyl derivatives of cyclodextrins on the enzymatic decomposition of l-tryptophan by l-tryptophan indole-lyase
Carbohydr. Res.
344
304-130
2008
Escherichia coli
Yang, R.; Cruz-Vera, L.R.; Yanofsky, C.
23S rRNA nucleotides in the peptidyl transferase center are essential for tryptophanase operon induction
J. Bacteriol.
191
3445-3450
2009
Escherichia coli
hang, Y.; Hong, G.
Evidences of Hfq associates with tryptophanase and affects extracellular indole levels
Acta Biochim. Biophys. Sin.
41
709-717
2009
Escherichia coli
Kogan, A.; Gdalevsky, G.Y.; Cohen-Luria, R.; Goldgur, Y.; Phillips, R.S.; Parola, A.H.; Almog, O.
Conformational changes and loose packing promote E. coli tryptophanase cold lability
BMC Struct. Biol.
9
65
2009
Escherichia coli (P0A853), Escherichia coli, Escherichia coli SVS 370 (P0A853)
Wigginton, N.S.; Titta, A.; Piccapietra, F.; Dobias, J.; Nesatyy, V.J.; Suter, M.J.; Bernier-Latmani, R.
Binding of silver nanoparticles to bacterial proteins depends on surface modifications and inhibits enzymatic activity
Environ. Sci. Technol.
44
2163-2168
2010
Escherichia coli
Shimada, A.; Ozaki, H.; Saito, T.; Noriko, F.
Tryptophanase-catalyzed L-tryptophan synthesis from D-serine in the presence of diammonium hydrogen phosphate
Int. J. Mol. Sci.
10
2578-2590
2009
Escherichia coli
Chi, F.; Wang, Y.; Gallaher, T.K.; Wu, C.H.; Jong, A.; Huang, S.H.
Identification of IbeR as a stationary-phase regulator in meningitic Escherichia coli K1 that carries a loss-of-function mutation in rpoS
J. Biomed. Biotechnol.
2009
520283
2009
Escherichia coli, Escherichia coli K1
Scherzer, R.; Gdalevsky, G.; Goldgur, Y.; Cohen-Luria, R.; Bittner, S.; Parola, A.
New tryptophanase inhibitors: Towards prevention of bacterial biofilm formation
J. Enzyme Inhib. Med. Chem.
24
350-355
2009
Escherichia coli
Hirakawa, H.; Kodama, T.; Takumi-Kobayashi, A.; Honda, T.; Yamaguchi, A.
Secreted indole serves as a signal for expression of type III secretion system translocators in enterohaemorrhagic Escherichia coli O157:H7
Microbiology
155
541-550
2009
Escherichia coli, Escherichia coli O157:H7 Sakai
Yoshida, Y.; Sasaki, T.; Ito, S.; Tamura, H.; Kunimatsu, K.; Kato, H.
Identification and molecular characterization of tryptophanase encoded by tnaA in Porphyromonas gingivalis
Microbiology
155
968-978
2009
Porphyromonas gingivalis, Porphyromonas gingivalis W83
Kuczynska-Wisnik, D.; Matuszewska, E.; Laskowska, E.
Escherichia coli heat-shock proteins IbpA and IbpB affect biofilm formation by influencing the level of extracellular indole
Microbiology
156
148-157
2010
Escherichia coli
An, H.M.; Baek, E.H.; Jang, S.; Lee, d.o..K.; Kim, M.J.; Kim, J.R.; Lee, K.O.; Park, J.G.; Ha, N.J.
Efficacy of Lactic Acid Bacteria (LAB) supplement in management of constipation among nursing home residents
Nutr. J.
9
5-5
2010
Homo sapiens
Phillips, R.S.; Ghaffari, R.; Dinh, P.; Lima, S.; Bartlett, D.
Properties of tryptophan indole-lyase from a piezophilic bacterium, Photobacterium profundum SS9
Arch. Biochem. Biophys.
506
35-41
2011
Escherichia coli, Photobacterium profundum (Q6LP64), Photobacterium profundum, Photobacterium profundum SS9 (Q6LP64), Photobacterium profundum SS9
Sasaki-Imamura, T.; Yoshida, Y.; Suwabe, K.; Yoshimura, F.; Kato, H.
Molecular basis of indole production catalyzed by tryptophanase in the genus Prevotella
FEMS Microbiol. Lett.
322
51-59
2011
Prevotella intermedia (E9RK37), Prevotella intermedia, Prevotella intermedia ATCC 25611 (E9RK37)
Bhatt, S.; Anyanful, A.; Kalman, D.
CsrA and TnaB coregulate tryptophanase activity to promote exotoxin-induced killing of Caenorhabditis elegans by enteropathogenic Escherichia coli
J. Bacteriol.
193
4516-4522
2011
Escherichia coli
Shimada, A.; Ozaki, H.; Saito, T.; Fujii, N.
Reaction pathway of tryptophanase-catalyzed L-tryptophan synthesis from D-serine
J. Chromatogr. B
879
3289-3295
2011
Escherichia coli
Hara, R.; Kino, K.
Enhanced synthesis of 5-hydroxy-L-tryptophan through tetrahydropterin regeneration
AMB Express
3
70
2013
Escherichia coli
Phillips, R.S.; Kalu, U.; Hay, S.
Evidence of preorganization in quinonoid intermediate formation from L-Trp in H463F mutant Escherichia coli tryptophan indole-lyase from effects of pressure and pH
Biochemistry
51
6527-6533
2012
Escherichia coli
Harris, A.P.; Phillips, R.S.
Benzimidazole analogs of (L)-tryptophan are substrates and inhibitors of tryptophan indole lyase from Escherichia coli
FEBS J.
280
1807-1817
2013
Escherichia coli, Escherichia coli JM109
Li, G.; Young, K.D.
Indole production by the tryptophanase TnaA in Escherichia coli is determined by the amount of exogenous tryptophan
Microbiology
159
402-410
2013
Escherichia coli, Escherichia coli MG1655
Du, J.; Duan, J.J.; Zhang, Q.; Hou, J.; Bai, F.; Chen, N.; Bai, G.
Enzymatic synthesis of L-tryptophan from D,L-2-amino-delta2-thiazoline-4-carboxylic acid and indole by Pseudomonas sp. TS1138 L-2-amino-delta2-thiazoline-4-carboxylic acid hydrolase, S-carbamyl-L-cysteine amidohydrolase, and Escherichia coli L-tryptophanase
Prikl. Biokhim. Mikrobiol.
48
183-190
2012
Escherichia coli
Phillips, R.S.; Buisman, A.A.; Choi, S.; Hussaini, A.; Wood, Z.A.
The crystal structure of Proteus vulgaris tryptophan indole-lyase complexed with oxindolyl-L-alanine implications for the reaction mechanism
Acta Crystallogr. Sect. D
74
748-759
2018
Escherichia coli (P0A853), Escherichia coli, Proteus vulgaris (P28796), Proteus vulgaris
Rety, S.; Deschamps, P.; Leulliot, N.
Structure of Escherichia coli tryptophanase purified from an alkaline-stressed bacterial culture
Acta Crystallogr. Sect. F
71
1378-1383
2015
Escherichia coli (P0A853), Escherichia coli
Kogan, A.; Raznov, L.; Gdalevsky, G.; Cohen-Luria, R.; Almog, O.; Parola, A.; Goldgur, Y.
Structures of Escherichia coli tryptophanase in holo and semi-holo forms
Acta Crystallogr. Sect. F
71
286-290
2015
Escherichia coli (P0A853), Escherichia coli
Xu, Y.; Zhang, Z.; Ali, M.M.; Sauder, J.; Deng, X.; Giang, K.; Aguirre, S.D.; Pelton, R.; Li, Y.; Filipe, C.D.
Turning tryptophanase into odor-generating biosensors
Angew. Chem. Int. Ed. Engl.
53
2620-2622
2014
Escherichia coli (P0A853)
Nuidate, T.; Tansila, N.; Chomchuen, P.; Phattaranit, P.; Eangchuan, S.; Vuddhakul, V.
Characterization of tryptophanase from Vibrio cholerae
Appl. Biochem. Biotechnol.
175
243-252
2015
Vibrio cholerae O1 (A5EYI0), Vibrio cholerae O1 ATCC 39541 (A5EYI0)
Watsuji, T.O.; Takano, H.; Yamabe, T.; Tamazawa, S.; Ikemura, H.; Ohishi, T.; Matsuda, T.; Shiratori-Takano, H.; Beppu, T.; Ueda, K.
Analysis of the tryptophanase expression in Symbiobacterium thermophilum in a coculture with Geobacillus stearothermophilus
Appl. Microbiol. Biotechnol.
98
10177-10186
2014
Symbiobacterium thermophilum (P31015), Symbiobacterium thermophilum, Symbiobacterium thermophilum T / IAM 14863 / JCM 14929 (P31015)
Do, Q.T.; Nguyen, G.T.; Celis, V.; Phillips, R.S.
Inhibition of Escherichia coli tryptophan indole-lyase by tryptophan homologues
Arch. Biochem. Biophys.
560
20-26
2014
Escherichia coli (P0A853), Escherichia coli
Faleev, N.G.; Zakomirdina, L.N.; Vorobev, M.M.; Tsvetikova, M.A.; Gogoleva, O.I.; Demidkina, T.V.; Phillips, R.S.
A straightforward kinetic evidence for coexistence of induced fit and selected fit in the reaction mechanism of a mutant tryptophan indole lyase Y72F from Proteus vulgaris
Biochim. Biophys. Acta
1844
1860-1867
2014
Proteus vulgaris (P28796), Proteus vulgaris
Phillips, R.S.; Demidkina, T.V.; Faleev, N.G.
The role of substrate strain in the mechanism of the carbon-carbon lyases
Bioorg. Chem.
57
198-205
2014
Escherichia coli (P0A853), Proteus vulgaris (P28796)
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