26:
245:
HycI is involved in processing of pre-HycE (the large subunit of hydrogenase 3),; HybD is involved in processing of pre-HybC (the large subunit of hydrogenase 2); and HyaD is assumed to be involved in processing of the large subunit of hydrogenase 1.
529:
Theodoratou E, Paschos A, Mintz-Weber, Bock A (February 2000). "Analysis of the cleavage site specificity of the endopeptidase involved in the maturation of the large subunit of hydrogenase 3 from
Escherichia coli".
493:
Rossmann R, Sauter M, Lottspeich F, Bock A (March 1994). "Maturation of the large subunit (HYCE) of
Escherichia coli hydrogenase 3 requires nickel incorporation followed by C-terminal processing at Arg537".
261:. This cleavage occurs only in the presence of nickel, and the endopeptidase probably uses the metal in the large subunit of -hydrogenases as a recognition motif. There is no direct evidence for the
455:
Theodoratou E, Paschos A, Magalon A, Fritsche E, Huber R, Bock A (April 2000). "Nickel serves as a substrate recognition motif for the endopeptidase involved in hydrogenase maturation".
283:
for members of this family: HycI, HybD, HyaD, HoxM, HoxW, HupD, HynC, HupM, VhoD, VhtD. Gene/protein names are sometimes used interchangeably to designate various "hydrogenase cluster"
150:
576:
Fritsche E, Paschos A, Beisel HG, Bock A, Huber R (May 1999). "Crystal structure of the hydrogenase maturating endopeptidase HYBD from
Escherichia coli".
98:
382:
Blokesch M, Paschos A, Theodoratou E, Bauer A, Hube M, Huth S, Bock A (August 2002). "Metal insertion into NiFe-hydrogenases".
170:
291:. For example, the following names are used for members of this group, but also for unrelated proteins: HupD is used in
301:
species to designate an unrelated hydrogenase maturation factor; HydD is used to designate hydrogenase structural
680:
266:
158:
191:
611:
Menon NK, Robbins J, Der
Vartanian M, Patil D, Peck HD, Menon AL, Robson RL, Przybyla AE (September 1993).
307:
154:
232:
111:
642:
555:
217:
634:
593:
547:
511:
472:
434:
399:
364:
270:
213:
145:
624:
585:
539:
503:
464:
426:
391:
356:
241:
417:
Maroney MJ (April 1999). "Structure/function relationships in nickel metallobiochemistry".
137:
91:
507:
324:
209:
187:
430:
360:
674:
629:
612:
468:
103:
646:
54:
559:
276:
133:
67:
666:
613:"Carboxy-terminal processing of the large subunit of [NiFe] hydrogenases"
79:
262:
225:
202:
236:
288:
250:
239:
end by the corresponding hydrogenase maturation endopeptidase. For example,
228:
216:
devoid of the metalloenzyme active site. This precursor undergoes a complex
597:
589:
551:
476:
438:
403:
368:
638:
543:
515:
107:
25:
662:
297:
284:
280:
254:
74:
395:
258:
221:
206:
195:
165:
86:
347:
Casalot L, Rousset M (May 2001). "Maturation of the hydrogenases".
302:
658:
224:. At one step of this process, after nickel incorporation, each
127:
61:
49:
269:-binding site, but there are predictions based on an available
220:
maturation process that requires a number of accessory
657:
This article incorporates text from the public domain
30:
hydrogenase maturating endopeptidase hybd from e. coli
164:
144:
126:
121:
97:
85:
73:
60:
48:
40:
35:
18:
279:note: the following names are used in different
571:
569:
450:
448:
342:
340:
488:
486:
8:
118:
24:
628:
336:
184:hydrogenase maturation protease family
15:
7:
287:unrelated to each other in various
508:10.1111/j.1432-1033.1994.tb18634.x
14:
469:10.1046/j.1432-1327.2000.01202.x
19:Hydrogenase maturation protease
1:
431:10.1016/S1367-5931(99)80032-5
361:10.1016/S0966-842X(01)02009-1
249:The cleavage site is after a
122:Available protein structures:
630:10.1016/0014-5793(93)80303-C
697:
656:
182:In molecular biology, the
117:
23:
293:Azotobacter chroococcum
192:aspartic endopeptidases
590:10.1006/jmbi.1999.2719
308:Thermococcus litoralis
212:, is synthesized as a
201:The large subunit of -
544:10.1007/s002039900116
315:, and other species.
257:, liberating a short
233:proteolytic cleavage
419:Curr Opin Chem Biol
384:Biochem. Soc. Trans
205:, as well as other
396:10.1042/bst0300674
218:post-translational
325:MEROPS family A31
313:Pyrococcus abyssi
180:
179:
176:
175:
171:structure summary
688:
651:
650:
632:
608:
602:
601:
573:
564:
563:
526:
520:
519:
490:
481:
480:
452:
443:
442:
414:
408:
407:
379:
373:
372:
349:Trends Microbiol
344:
242:Escherichia coli
231:is processed by
119:
28:
16:
696:
695:
691:
690:
689:
687:
686:
685:
681:Protein domains
671:
670:
669:
655:
654:
610:
609:
605:
575:
574:
567:
532:Arch. Microbiol
528:
527:
523:
496:Eur. J. Biochem
492:
491:
484:
457:Eur. J. Biochem
454:
453:
446:
416:
415:
411:
381:
380:
376:
346:
345:
338:
333:
321:
31:
12:
11:
5:
694:
692:
684:
683:
673:
672:
653:
652:
603:
565:
521:
482:
444:
409:
374:
335:
334:
332:
329:
328:
327:
320:
319:External links
317:
210:metalloenzymes
178:
177:
174:
173:
168:
162:
161:
148:
142:
141:
131:
124:
123:
115:
114:
101:
95:
94:
89:
83:
82:
77:
71:
70:
65:
58:
57:
52:
46:
45:
42:
38:
37:
33:
32:
29:
21:
20:
13:
10:
9:
6:
4:
3:
2:
693:
682:
679:
678:
676:
668:
664:
660:
648:
644:
640:
636:
631:
626:
623:(1–2): 91–5.
622:
618:
614:
607:
604:
599:
595:
591:
587:
584:(5): 989–98.
583:
579:
572:
570:
566:
561:
557:
553:
549:
545:
541:
537:
533:
525:
522:
517:
513:
509:
505:
502:(2): 377–84.
501:
497:
489:
487:
483:
478:
474:
470:
466:
463:(7): 1995–9.
462:
458:
451:
449:
445:
440:
436:
432:
428:
425:(2): 188–99.
424:
420:
413:
410:
405:
401:
397:
393:
390:(4): 674–80.
389:
385:
378:
375:
370:
366:
362:
358:
355:(5): 228–37.
354:
350:
343:
341:
337:
330:
326:
323:
322:
318:
316:
314:
310:
309:
304:
300:
299:
294:
290:
286:
282:
278:
274:
272:
268:
264:
260:
256:
252:
247:
244:
243:
238:
234:
230:
227:
223:
219:
215:
211:
208:
204:
199:
197:
194:belonging to
193:
189:
185:
172:
169:
167:
163:
160:
156:
152:
149:
147:
143:
139:
135:
132:
129:
125:
120:
116:
113:
109:
105:
102:
100:
96:
93:
90:
88:
84:
81:
78:
76:
72:
69:
66:
63:
59:
56:
53:
51:
47:
43:
39:
34:
27:
22:
17:
620:
616:
606:
581:
578:J. Mol. Biol
577:
538:(2): 110–6.
535:
531:
524:
499:
495:
460:
456:
422:
418:
412:
387:
383:
377:
352:
348:
312:
306:
296:
292:
277:Nomenclature
275:
248:
240:
200:
198:family A31.
183:
181:
263:active site
226:hydrogenase
203:hydrogenase
36:Identifiers
331:References
237:C-terminal
134:structures
667:IPR000671
617:FEBS Lett
289:organisms
281:organisms
271:structure
267:substrate
229:isoenzyme
214:precursor
80:IPR000671
675:Category
663:InterPro
647:39302159
598:10331925
552:10795682
477:10727938
439:10226043
404:12196162
369:11336840
298:Anabaena
285:proteins
222:proteins
151:RCSB PDB
75:InterPro
639:8405419
560:5613272
516:8125094
259:peptide
235:at the
55:PF01750
645:
637:
596:
558:
550:
514:
475:
437:
402:
367:
253:or an
207:nickel
196:MEROPS
188:family
166:PDBsum
140:
130:
112:SUPFAM
87:MEROPS
68:CL0095
41:Symbol
643:S2CID
556:S2CID
303:genes
186:is a
108:SCOPe
99:SCOP2
661:and
659:Pfam
635:PMID
594:PMID
548:PMID
512:PMID
473:PMID
435:PMID
400:PMID
365:PMID
295:and
159:PDBj
155:PDBe
138:ECOD
128:Pfam
104:1cfz
64:clan
62:Pfam
50:Pfam
44:HycI
625:doi
621:331
586:doi
582:288
540:doi
536:173
504:doi
500:220
465:doi
461:267
427:doi
392:doi
357:doi
305:in
265:or
255:Arg
251:His
190:of
146:PDB
92:A31
677::
665::
641:.
633:.
619:.
615:.
592:.
580:.
568:^
554:.
546:.
534:.
510:.
498:.
485:^
471:.
459:.
447:^
433:.
421:.
398:.
388:30
386:.
363:.
351:.
339:^
311:,
273:.
157:;
153:;
136:/
110:/
106:/
649:.
627::
600:.
588::
562:.
542::
518:.
506::
479:.
467::
441:.
429::
423:3
406:.
394::
371:.
359::
353:9
Text is available under the Creative Commons Attribution-ShareAlike License. Additional terms may apply.
