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Information on EC 3.7.1.13 - 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase for references in articles please use BRENDA:EC3.7.1.13Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The enzyme appears in viruses and cellular organisms
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2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate hydrolase
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(2E,4E)-6-(2-aminophenyl)-2-hydroxy-6-oxohexa-2,4-dienoate + H2O = anthranilate + (2E)-2-hydroxypenta-2,4-dienoate
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carbazole degradation
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Microbial metabolism in diverse environments
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(2E,4E)-6-(2-aminophenyl)-2-hydroxy-6-oxohexa-2,4-dienoate acylhydrolase
This enzyme catalyses the third step in the aerobic degradation pathway of carbazole. The effect of the presence of an amino group or hydroxyl group at the 2-position of the substrate is small. The enzyme has no cofactor requirement [2].
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CarC
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HOPDA hydrolase
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Q84II3
UniProt
brenda
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UniProt
brenda
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brenda
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UniProt
brenda
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2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid + H2O
benzoic acid + 2-hydroxypenta-2,4-dienoic acid
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate + H2O
anthranilate + 2-hydroxypenta-2,4-dienoate
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate + H2O
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2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
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2-hydroxy-6-oxohepta-2,4-dienoic acid + H2O
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2-hydroxymuconic semialdehyde + H2O
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additional information
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2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid + H2O
benzoic acid + 2-hydroxypenta-2,4-dienoic acid
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2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid + H2O
benzoic acid + 2-hydroxypenta-2,4-dienoic acid
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2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate + H2O
anthranilate + 2-hydroxypenta-2,4-dienoate
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2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate + H2O
anthranilate + 2-hydroxypenta-2,4-dienoate
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2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate + H2O
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2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate + H2O
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2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
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Q84II3
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2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
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2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
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2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
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2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
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2-hydroxy-6-oxohepta-2,4-dienoic acid + H2O
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Q84II3
0.56% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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2-hydroxy-6-oxohepta-2,4-dienoic acid + H2O
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0.38% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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2-hydroxy-6-oxohepta-2,4-dienoic acid + H2O
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0.38% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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2-hydroxymuconic semialdehyde + H2O
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Q84II3
0.49% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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2-hydroxymuconic semialdehyde + H2O
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0.54% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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2-hydroxymuconic semialdehyde + H2O
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0.54% of the activity with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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additional information
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hydrolytic activity decreases in the substrate order of 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate, 2-hydroxy-6-oxo-6-(2'-hydroxyphenyl)hexa-2,4-dienoate. Poor substrates: 2-hydroxy-6-oxohepta-2,4-dienoic acid, 2-hydroxymuconic semialdehyde
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additional information
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hydrolytic activity decreases in the substrate order of 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoate, 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate, 2-hydroxy-6-oxo-6-(2'-hydroxyphenyl)hexa-2,4-dienoate. Poor substrates: 2-hydroxy-6-oxohepta-2,4-dienoic acid, 2-hydroxymuconic semialdehyde
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additional information
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no cofactor requirement
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0.0046
2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid
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pH 7.5, 25°C
0.00251 - 0.00273
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
0.00251
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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pH 7.5, 25°C
0.00251
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
pH 7.5, 25°C
0.00273
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
Q84II3
pH 7.5, 25°C
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1300
2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid
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pH 7.5, 25°C
1.99 - 2.14
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
1.99
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
Q84II3
pH 7.5, 25°C
2.1
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
pH 7.5, 25°C
2.14
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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pH 7.5, 25°C
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730 - 852
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
730
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
Q84II3
pH 7.5, 25°C
852
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
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pH 7.5, 25°C
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9
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about 50% of maximal activity
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31000
2 * 31000, SDS-PAGe, 2 * 31300, calculated
31300
2 * 31000, SDS-PAGe, 2 * 31300, calculated
32231
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x * 32231, calculated, x * 33000, SDS-PAGE
33000
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x * 32231, calculated, x * 33000, SDS-PAGE
33000
Q84II3
2 * 33000, SDS-PAGE
33000
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2 * 33000, SDS-PAGE
70000
Q84II3
gel filtration
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x * 32231, calculated, x * 33000, SDS-PAGE
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x * 32231, calculated, x * 33000, SDS-PAGE
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dimer
Q84II3
2 * 33000, SDS-PAGE
dimer
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2 * 33000, SDS-PAGE
dimer
2 * 31000, SDS-PAGe, 2 * 31300, calculated
dimer
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2 * 31000, SDS-PAGe, 2 * 31300, calculated; 2 * 33000, SDS-PAGE
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to 1.86 A resolution, space group I422. The subunit of ht-CarCJ3 is divided into two domains, i.e., the core domain with residues 15-144 and 209-282, and the lid domain with residues 145-208. The invisible 10 amino acid residues Ile146-Asn155 correspond to the helix alpha4, which is the putative first alpha-helix in the lid domain. Sidechains of the active-site residues, Ser114 and His261, are clearly shown in the electron density map
Q84II3
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55
10 min, 75% residual activity
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recombinant enzyme
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recombinant enzyme
Q84II3
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expression in Escherichia coli
expression in Escherichia coli
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expression in Escherichia coli
Q84II3
expression in Escherichia coli
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S114A
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mutation in active-site serine. Approximately 40fold reduction in activity for the His-tagged mutant hydrolase relative to similar lysates of His-tagged native CarC
S114A
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mutation in active-site serine. Approximately 40fold reduction in activity for the His-tagged mutant hydrolase relative to similar lysates of His-tagged native CarC
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CARC_PSERE
290
32252
Swiss-Prot
A0A136WI62_9FIRM
314
34937
TrEMBL
A0A1J5SWH9_9ZZZZ
287
32362
TrEMBL
A0A2J7VDM9_9BURK
425
46083
TrEMBL
A0A0D5BMU8_ELIMR
548
62188
TrEMBL
A0A200GYY1_MYCPC
273
29295
TrEMBL
A0A1S1H6L1_9SPHN
275
29802
TrEMBL
A0A0K6MH61_BACIU
279
32319
TrEMBL
A0A0H4VVG5_9BORD
252
27487
TrEMBL
A0A1V5J5G2_9DELT
145
15900
TrEMBL
A0A0U5PQE1_9CLOT
316
35139
TrEMBL
A0A1A8T2C4_9GAMM
293
32438
TrEMBL
A0A0K6JJC0_BACCE
273
31261
TrEMBL
A0A2H5Z7B8_9BACT
279
30780
TrEMBL
A0A0X8WUV3_9CYAN
298
32735
TrEMBL
A0A110AXB5_9CYAN
295
32958
TrEMBL
A0A0U5JB83_9CLOT
320
36989
TrEMBL
A0A1S1NGH7_9MYCO
271
29346
TrEMBL
A0A2N7RBY5_9PSED
300
34554
TrEMBL
A0A0J6VER2_9MYCO
292
31797
TrEMBL
A0A2P8B5C2_9ACTN
294
31582
TrEMBL
A0A1Q9NVK8_9ARCH
315
36485
TrEMBL
A0A1E3AZS4_9FIRM
314
35739
TrEMBL
A0A2N7RKM3_9BURK
336
35981
TrEMBL
A0A1A9GJK3_9ACTN
272
28137
TrEMBL
A0A163XG67_9SYNE
325
35955
TrEMBL
A0A1Y2MKF7_PSEAH
279
29976
TrEMBL
A0A1X9M907_9BACI
298
33264
TrEMBL
A0A2H5VF74_9ARCH
258
29378
TrEMBL
A0A2S9XMJ9_9BACI
279
32259
TrEMBL
A0A2P4UM30_9ACTN
302
32026
TrEMBL
A0A1J5RNX7_9ZZZZ
312
35042
TrEMBL
A0A2P8A7G8_9ACTN
418
43792
TrEMBL
A0A2H6H9B2_9BACT
223
23747
TrEMBL
A0A181CAW1_9PROT
296
31953
TrEMBL
A0A0B7D528_PSEFL
300
34608
TrEMBL
A0A1V5TAH5_9SPIR
310
33173
TrEMBL
A0A0J6WFY8_9MYCO
283
30319
TrEMBL
A0A2S6R0U3_9PROT
302
33179
TrEMBL
A0A2H6H3B0_9BACT
241
26038
TrEMBL
A0A221UXF1_9FLAO
254
28767
TrEMBL
A0A1V5HCU0_9DELT
282
30930
TrEMBL
A0A0J6W1D7_9MYCO
295
32132
TrEMBL
A0A100JK19_STRSC
415
43285
TrEMBL
A0A1Y5ZM41_BACCE
271
31367
TrEMBL
A0A2J7VAF2_9BURK
425
46310
TrEMBL
A0A0U5LSC7_STRRE
419
44047
TrEMBL
A0A143XR11_9BACT
292
31755
TrEMBL
A0A0X8VBH1_CLOPR
314
35290
TrEMBL
A0A1Y5Z795_BACCE
279
32159
TrEMBL
A0A0X8WSB3_9CYAN
318
35522
TrEMBL
A0A0L6ZBD7_9CLOT
273
31267
TrEMBL
A0A143QDF1_9NOCA
302
32620
TrEMBL
A0A2S6QAQ2_9PROT
288
31972
TrEMBL
A0A0J6WQU8_9MYCO
292
31829
TrEMBL
A0A0N9YH63_9ARCH
268
30315
TrEMBL
A0A2S6WZU1_9ACTN
419
43794
TrEMBL
A0A2H5V8S4_9ARCH
267
30483
TrEMBL
A0A0N9Y611_9ARCH
275
32081
TrEMBL
A0A2W1JPF7_9CYAN
263
28953
TrEMBL
A0A164CRI7_9SYNE
321
35847
TrEMBL
A0A163RZM8_PROMR
295
32921
TrEMBL
A0A2H5YDS4_9BACT
85
9435
TrEMBL
A0A1V5HKM8_9BACT
247
27973
TrEMBL
A0A1V4IHV9_9CLOT
278
31431
TrEMBL
A0A0J6VB91_9MYCO
296
32473
TrEMBL
A0A1Y5YVQ4_BACCE
279
32142
TrEMBL
A0A1V5L794_9PROT
238
27170
TrEMBL
A0A1E3A887_9FIRM
314
35721
TrEMBL
A0A2W1JPN4_9CYAN
297
32997
TrEMBL
A0A202FTA2_MYCPC
287
31320
TrEMBL
A0A0F0CN13_9CLOT
316
35195
TrEMBL
A0A161IA64_9MICO
263
27630
TrEMBL
A0A0U5P5S6_9CLOT
315
35581
TrEMBL
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Riddle, R.R.; Gibbs, P.R.; Willson, R.C.; Benedik, M.J.
Purification and properties of 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid hydrolase involved in microbial degradation of carbazole
Protein Expr. Purif.
28
182-189
2003
Pseudomonas sp., Pseudomonas sp. LD2
brenda
Habe, H.; Morii, K.; Fushinobu, S.; Nam, J.W.; Ayabe, Y.; Yoshida, T.; Wakagi, T.; Yamane, H.; Nojiri, H.; Omori, T.
Crystal structure of a histidine-tagged serine hydrolase involved in the carbazole degradation (CarC enzyme)
Biochem. Biophys. Res. Commun.
303
631-639
2003
Janthinobacterium sp. J3 (Q84II3), Pseudomonas resinovorans, Pseudomonas resinovorans CA10
brenda
Nojiri, H.; Taira, H.; Iwata, K.; Morii, K.; Nam, J.W.; Yoshida, T.; Habe, H.; Nakamura, S.; Shimizu, K.; Yamane, H.; Omori, T.
Purification and characterization of meta-cleavage compound hydrolase from a carbazole degrader Pseudomonas resinovorans strain CA10
Biosci. Biotechnol. Biochem.
67
36-45
2003
Pseudomonas resinovorans (Q9AQM4), Pseudomonas resinovorans CA10 (Q9AQM4)
brenda
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