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IUBMB Comments A heme-thiolate (P-450) enzyme from the bacterium Bacillus subtilis. The order of events during the overall reaction is unknown. Pulcherrimic acid spontaneously forms an iron chelate with Fe(3+) to form the red pigment pulcherrimin .
The enzyme appears in viruses and cellular organisms
Synonyms
cyp134a1, pulcherriminic acid synthase,
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cyclo-L-leucyl-L-leucyl dipeptide oxidase
cyclo-L-leucyl-L-leucyl dipeptide oxidase
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cyclo-L-leucyl-L-leucyl dipeptide oxidase
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CYP134A1
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CypX
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ambiguous
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cyclo(L-leucyl-L-leucyl) + 6 reduced ferredoxin + 3 O2 = pulcherriminic acid + 6 oxidized ferredoxin + 4 H2O
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cyclo(L-leucyl-L-leucyl),reduced-ferredoxin:oxygen oxidoreductase (N-hydroxylating,aromatizing)
A heme-thiolate (P-450) enzyme from the bacterium Bacillus subtilis. The order of events during the overall reaction is unknown. Pulcherrimic acid spontaneously forms an iron chelate with Fe(3+) to form the red pigment pulcherrimin [2].
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1-phenylimidazole + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
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?
2,5-di-tert-butylhydroquinone + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
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?
2,5-di-tert-butylquinone + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
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-
?
2-phenylimidazole + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
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?
4-phenylimidazole + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
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-
?
cyclo(L-alanyl-L-alanyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
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?
cyclo(L-leucyl-L-leucyl) + reduced ferredoxin + O2
pulcherriminic acid + oxidized ferredoxin + H2O
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?
cyclo(L-leucyl-L-phenylalanyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
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?
cyclo(L-leucyl-L-prolyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
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?
cyclo(L-leucyl-L-tryptophanyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
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-
?
cyclo(L-methionyl-L-methionyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
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?
cyclo(L-valyl-L-valyl) + reduced ferredoxin + O2
? + oxidized ferredoxin + H2O
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?
additional information
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additional information
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the enzyme does not use dimethylpyrazine and tetramethylpyrazine as substrates
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?
additional information
?
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the enzyme does not use dimethylpyrazine and tetramethylpyrazine as substrates
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?
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cyclo(L-leucyl-L-leucyl) + reduced ferredoxin + O2
pulcherriminic acid + oxidized ferredoxin + H2O
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?
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ATCC 56775
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brenda
ATCC 56775
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brenda
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UniProt
brenda
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CYPX_BACSU
Bacillus subtilis (strain 168)
405
0
45473
Swiss-Prot
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A0A6I7BQ61_BACIU
405
0
45518
TrEMBL
-
A0A1Y2MHX9_STRPT
414
0
45503
TrEMBL
-
A0A0D0TJI9_PSEFL
741
0
82328
TrEMBL
-
A0A2K8P7Z9_STRLA
414
0
45133
TrEMBL
-
A0A5E6P838_PSEFL
425
0
46871
TrEMBL
-
A0A164TWH2_BACIU
405
0
45473
TrEMBL
-
A0A0Q1DT89_9CORY
402
0
45104
TrEMBL
-
A0A2P4UBX6_9ACTN
722
0
79523
TrEMBL
-
A0A1D2IH78_9ACTN
408
0
45073
TrEMBL
-
A0A1K2G0J6_9ACTN
408
0
45256
TrEMBL
-
A0A1D8FMH9_BACIU
405
0
45473
TrEMBL
-
A0A1B8YBC6_9GAMM
420
0
47582
TrEMBL
-
A0A1V2MT21_9ACTN
408
0
44581
TrEMBL
-
A0A5E7T520_PSEFL
425
0
47023
TrEMBL
-
A0A2K8PQE8_STRLA
407
0
45045
TrEMBL
-
A0A1Y6B2F8_BACCE
86
0
9593
TrEMBL
-
A0A1Y2NNC3_STRFR
411
0
45331
TrEMBL
-
A0A3N6HPT7_9ACTN
342
0
35631
TrEMBL
-
A0A1D8G7U3_9ACTN
411
0
45317
TrEMBL
-
A0A1C7DAD0_9SPHN
406
0
45988
TrEMBL
-
A0A127MWW0_9PSED
424
0
47094
TrEMBL
-
A0A2S6WHR5_9ACTN
407
0
45023
TrEMBL
-
A0A5B7UKB0_9ACTN
416
0
45679
TrEMBL
-
A0A654MY17_BACIU
405
0
45499
TrEMBL
-
A0A3N6EUD6_9ACTN
436
0
46906
TrEMBL
-
A0A4V0ZJD5_9ACTN
414
0
45922
TrEMBL
-
A0A5P9PM71_9PSEU
405
0
44830
TrEMBL
-
A0A5E7ENW3_PSEFL
375
0
40112
TrEMBL
-
A0A1B9EQS4_9ACTN
406
0
45022
TrEMBL
-
A0A1B9F053_9ACTN
348
0
36173
TrEMBL
-
A0A1D2IB24_9ACTN
416
0
44485
TrEMBL
-
A0A0D8BBV2_9ACTN
407
0
46047
TrEMBL
-
A0A6H0H7T4_BACIU
405
0
45473
TrEMBL
-
A0A3N6E6T9_9ACTN
389
0
40740
TrEMBL
-
A0A399GL02_9ACTN
408
0
45215
TrEMBL
-
A0A433DU31_9ACTN
406
0
45005
TrEMBL
-
A0A2R8BGE9_9RHOB
447
1
49175
TrEMBL
-
A0A3N6H667_9ACTN
413
0
46950
TrEMBL
-
A0A3N6EN73_9ACTN
410
0
44757
TrEMBL
-
A0A433DZ54_9ACTN
344
0
35943
TrEMBL
-
A0A2P8AH27_9ACTN
407
0
44917
TrEMBL
-
A0A1B2H4I9_STRNR
432
0
47454
TrEMBL
-
A0A1V2MW61_9ACTN
345
0
35821
TrEMBL
-
A0A3N6E3U7_9ACTN
406
0
44676
TrEMBL
-
A0A6H2EDZ7_BACIU
404
0
45371
TrEMBL
-
A0A3N6EXZ4_9ACTN
417
0
45754
TrEMBL
-
A0A2K8QX67_9ACTN
125
0
13081
TrEMBL
-
A0A3G4VLB2_9ACTN
406
0
44710
TrEMBL
-
A0A125QDN0_PSEFL
425
0
46845
TrEMBL
-
A0A3N6HDB8_9ACTN
406
0
45078
TrEMBL
-
A0A5E6PG59_PSEFL
425
0
47009
TrEMBL
-
A0A1B9EX95_9ACTN
413
0
45299
TrEMBL
-
A0A1Y6AT43_BACCE
86
0
9604
TrEMBL
-
A0A5Q2ZRP2_BACIU
405
0
45499
TrEMBL
-
A0A1Z3HQN0_9CYAN
469
0
53183
TrEMBL
-
A0A3N6ITM8_9ACTN
408
0
44887
TrEMBL
-
A0A5E6PLA3_PSEFL
425
0
47017
TrEMBL
-
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Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
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56300
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x * 56300, calculated from amino acid sequence
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?
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x * 56300, calculated from amino acid sequence
?
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x * 56300, calculated from amino acid sequence
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mutant enzyme A356T, hanging drop vapor diffusion method, using 0.1 M Bis-Tris (pH 6.5), 0.1 M MgCl2, 12% (w/v) polyethylene glycol 3350
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A356T
mutant enzyme A356T crystallizes under several PEG-3350 conditions, with an optimum pH around 6 and a relatively low PEG concentration (12-15% (w/v)). The wild-type protein does not crystallize under these conditions, while the protein of the A356T mutant crystallizes readily and forms large, thin plates
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Ni-NTA column chromatography, Resource Q column chromatography, and Superose-12 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
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Yu, J.; Chang, P.K.; Bhatnagar, D.; Cleveland, T.E.
Genes encoding cytochrome P450 and monooxygenase enzymes define one end of the aflatoxin pathway gene cluster in Aspergillus parasiticus
Appl. Microbiol. Biotechnol.
53
583-590
2000
Aspergillus parasiticus, Aspergillus parasiticus SRRC 143
brenda
Cryle, M.J.; Bell, S.G.; Schlichting, I.
Structural and biochemical characterization of the cytochrome P450 CypX (CYP134A1) from Bacillus subtilis: a cyclo-L-leucyl-L-leucyl dipeptide oxidase
Biochemistry
49
7282-7296
2010
Bacillus subtilis (O34926), Bacillus subtilis
brenda
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1.14.15.13 pulcherriminic acid synthase
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