Knowledge

Catechol dioxygenase

Source đź“ť

109: 644: 188: 669: 282: 363: 161: 147: 519: 272: 248: 234: 181: 287: 243: 229: 634: 504: 620: 607: 594: 581: 568: 555: 542: 321: 302: 257: 214: 514: 468: 411: 205: 68: 61: 57: 50: 46: 38: 91:
xylE gene, which encodes catechol 2,3-dioxygenase, is often used as a reporter to quantitate gene expression.
416: 174: 121: 437: 356: 509: 277: 664: 473: 406: 330: 292: 87: 108: 157: 143: 452: 447: 421: 349: 166: 499: 483: 396: 648: 537: 478: 197: 94:
An example of the reaction carried out by catechol 1,2-dioxygenase is the formation of
42: 23: 658: 442: 401: 391: 224: 95: 615: 550: 386: 643: 311: 589: 563: 201: 126: 79: 154:
The biological chemistry of the elements: The inorganic chemistry of life
102: 71: 64: 53: 34: 30: 74:). The active site of catechol dioxygenases most frequently contains 602: 372: 252: 238: 26: 576: 107: 75: 345: 170: 45:
and have several different substrate specificities, including
341: 632: 528: 492: 461: 430: 379: 320: 301: 213: 41:. Catechol dioxygenases belong to the class of 156:, 2nd Edition, Oxford University Press, 2001, 357: 182: 152:J.J.R. FraĂşsto da Silva and R.J.P. Williams, 8: 364: 350: 342: 189: 175: 167: 29:that carry out the oxidative cleavage of 67:), and protocatechuate 3,4-dioxygenase ( 639: 33:. This class of enzymes incorporate 7: 140:Principles of Bioinorganic Chemistry 138:Stephen J. Lippard, Jeremy M. Berg, 283:4-Hydroxyphenylpyruvate dioxygenase 142:, University Science Books, 1994, 82:-containing forms are also known. 14: 642: 1: 273:Homogentisate 1,2-dioxygenase 249:Arachidonate 15-lipoxygenase 235:Arachidonate 12-lipoxygenase 288:Indoleamine 2,3-dioxygenase 244:Arachidonate 8-lipoxygenase 230:Arachidonate 5-lipoxygenase 686: 670:Natural phenols metabolism 520:Michaelis–Menten kinetics 258:Linoleate 11-lipoxygenase 412:Diffusion-limited enzyme 58:catechol 2,3-dioxygenase 47:catechol 1,2-dioxygenase 122:Bioinorganic chemistry 112: 505:Eadie–Hofstee diagram 438:Allosteric regulation 217:: two atoms of oxygen 111: 20:Catechol dioxygenases 515:Lineweaver–Burk plot 305:: one atom of oxygen 278:Cysteine dioxygenase 268:Catechol dioxygenase 474:Enzyme superfamily 407:Enzyme promiscuity 331:Inositol oxygenase 312:Firefly luciferase 293:Chlorite dismutase 265:other dioxygenase: 113: 88:Pseudomonas putida 630: 629: 339: 338: 677: 647: 646: 638: 510:Hanes–Woolf plot 453:Enzyme activator 448:Enzyme inhibitor 422:Enzyme catalysis 366: 359: 352: 343: 191: 184: 177: 168: 685: 684: 680: 679: 678: 676: 675: 674: 655: 654: 653: 641: 633: 631: 626: 538:Oxidoreductases 524: 500:Enzyme kinetics 488: 484:List of enzymes 457: 426: 397:Catalytic triad 375: 370: 340: 335: 316: 297: 209: 198:Oxidoreductases 195: 135: 118: 105:, shown below. 43:oxidoreductases 17: 12: 11: 5: 683: 681: 673: 672: 667: 657: 656: 652: 651: 628: 627: 625: 624: 611: 598: 585: 572: 559: 546: 532: 530: 526: 525: 523: 522: 517: 512: 507: 502: 496: 494: 490: 489: 487: 486: 481: 476: 471: 465: 463: 462:Classification 459: 458: 456: 455: 450: 445: 440: 434: 432: 428: 427: 425: 424: 419: 414: 409: 404: 399: 394: 389: 383: 381: 377: 376: 371: 369: 368: 361: 354: 346: 337: 336: 334: 333: 327: 325: 318: 317: 315: 314: 308: 306: 299: 298: 296: 295: 290: 285: 280: 275: 270: 261: 260: 255: 246: 241: 232: 220: 218: 211: 210: 202:monooxygenases 196: 194: 193: 186: 179: 171: 165: 164: 150: 134: 131: 130: 129: 124: 117: 114: 24:metalloprotein 16:Type of enzyme 15: 13: 10: 9: 6: 4: 3: 2: 682: 671: 668: 666: 663: 662: 660: 650: 645: 640: 636: 622: 618: 617: 612: 609: 605: 604: 599: 596: 592: 591: 586: 583: 579: 578: 573: 570: 566: 565: 560: 557: 553: 552: 547: 544: 540: 539: 534: 533: 531: 527: 521: 518: 516: 513: 511: 508: 506: 503: 501: 498: 497: 495: 491: 485: 482: 480: 479:Enzyme family 477: 475: 472: 470: 467: 466: 464: 460: 454: 451: 449: 446: 444: 443:Cooperativity 441: 439: 436: 435: 433: 429: 423: 420: 418: 415: 413: 410: 408: 405: 403: 402:Oxyanion hole 400: 398: 395: 393: 390: 388: 385: 384: 382: 378: 374: 367: 362: 360: 355: 353: 348: 347: 344: 332: 329: 328: 326: 323: 319: 313: 310: 309: 307: 304: 300: 294: 291: 289: 286: 284: 281: 279: 276: 274: 271: 269: 266: 263: 262: 259: 256: 254: 250: 247: 245: 242: 240: 236: 233: 231: 228: 226: 222: 221: 219: 216: 212: 207: 203: 199: 192: 187: 185: 180: 178: 173: 172: 169: 163: 162:0-19-850848-4 159: 155: 151: 149: 148:0-935702-72-5 145: 141: 137: 136: 132: 128: 125: 123: 120: 119: 115: 110: 106: 104: 100: 99:-muconic acid 98: 92: 90: 89: 83: 81: 77: 73: 70: 66: 63: 59: 55: 52: 48: 44: 40: 36: 32: 28: 25: 21: 616:Translocases 613: 600: 587: 574: 561: 551:Transferases 548: 535: 392:Binding site 267: 264: 225:lipoxygenase 223: 153: 139: 96: 93: 86: 84: 19: 18: 387:Active site 665:EC 1.13.11 659:Categories 590:Isomerases 564:Hydrolases 431:Regulation 133:References 469:EC number 127:Oxygenase 80:manganese 72:1.13.11.3 65:1.13.11.2 54:1.13.11.1 39:substrate 37:into the 31:catechols 493:Kinetics 417:Cofactor 380:Activity 116:See also 103:catechol 35:dioxygen 649:Biology 603:Ligases 373:Enzymes 324:: other 322:1.13.99 303:1.13.12 215:1.13.11 97:cis,cis 27:enzymes 635:Portal 577:Lyases 253:ALOX15 239:ALOX12 160:  146:  78:, but 529:Types 208:1.13) 101:from 621:list 614:EC7 608:list 601:EC6 595:list 588:EC5 582:list 575:EC4 569:list 562:EC3 556:list 549:EC2 543:list 536:EC1 158:ISBN 144:ISBN 85:The 76:iron 22:are 56:), 661:: 206:EC 200:: 69:EC 62:EC 51:EC 637:: 623:) 619:( 610:) 606:( 597:) 593:( 584:) 580:( 571:) 567:( 558:) 554:( 545:) 541:( 365:e 358:t 351:v 251:/ 237:/ 227:: 204:( 190:e 183:t 176:v 60:( 49:(

Index

metalloprotein
enzymes
catechols
dioxygen
substrate
oxidoreductases
catechol 1,2-dioxygenase
EC
1.13.11.1
catechol 2,3-dioxygenase
EC
1.13.11.2
EC
1.13.11.3
iron
manganese
Pseudomonas putida
cis,cis-muconic acid
catechol

Bioinorganic chemistry
Oxygenase
ISBN
0-935702-72-5
ISBN
0-19-850848-4
v
t
e
Oxidoreductases

Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.

↑