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Sequence of COLG_HATHI

EC Number:3.4.24.3

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
microbial collagenase
Q9X721
Hathewaya histolytica
1118
126242
Reaction
Digestion of native collagen in the triple helical region at -/-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'
Other sequences found for EC No. 3.4.24.3

General information:

Sequence
show sequence in fasta format
   0 MKKNILKILM DSYSKESKIQ TVRRVTSVSL LAVYLTMNTS SLVLAKPIEN TNDTSIKNVE
  60 KLRNAPNEEN SKKVEDSKND KVEHVKNIEE AKVEQVAPEV KSKSTLRSAS IANTNSEKYD
 120 FEYLNGLSYT ELTNLIKNIK WNQINGLFNY STGSQKFFGD KNRVQAIINA LQESGRTYTA
 180 NDMKGIETFT EVLRAGFYLG YYNDGLSYLN DRNFQDKCIP AMIAIQKNPN FKLGTAVQDE
 240 VITSLGKLIG NASANAEVVN NCVPVLKQFR ENLNQYAPDY VKGTAVNELI KGIEFDFSGA
 300 AYEKDVKTMP WYGKIDPFIN ELKALGLYGN ITSATEWASD VGIYYLSKFG LYSTNRNDIV
 360 QSLEKAVDMY KYGKIAFVAM ERITWDYDGI GSNGKKVDHD KFLDDAEKHY LPKTYTFDNG
 420 TFIIRAGDKV SEEKIKRLYW ASREVKSQFH RVVGNDKALE VGNADDVLTM KIFNSPEEYK
 480 FNTNINGVST DNGGLYIEPR GTFYTYERTP QQSIFSLEEL FRHEYTHYLQ ARYLVDGLWG
 540 QGPFYEKNRL TWFDEGTAEF FAGSTRTSGV LPRKSILGYL AKDKVDHRYS LKKTLNSGYD
 600 DSDWMFYNYG FAVAHYLYEK DMPTFIKMNK AILNTDVKSY DEIIKKLSDD ANKNTEYQNH
 660 IQELADKYQG AGIPLVSDDY LKDHGYKKAS EVYSEISKAA SLTNTSVTAE KSQYFNTFTL
 720 RGTYTGETSK GEFKDWDEMS KKLDGTLESL AKNSWSGYKT LTAYFTNYRV TSDNKVQYDV
 780 VFHGVLTDNA DISNNKAPIA KVTGPSTGAV GRNIEFSGKD SKDEDGKIVS YDWDFGDGAT
 840 SRGKNSVHAY KKAGTYNVTL KVTDDKGATA TESFTIEIKN EDTTTPITKE MEPNDDIKEA
 900 NGPIVEGVTV KGDLNGSDDA DTFYFDVKED GDVTIELPYS GSSNFTWLVY KEGDDQNHIA
 960 SGIDKNNSKV GTFKSTKGRH YVFIYKHDSA SNISYSLNIK GLGNEKLKEK ENNDSSDKAT
1020 VIPNFNTTMQ GSLLGDDSRD YYSFEVKEEG EVNIELDKKD EFGVTWTLHP ESNINDRITY
1080 GQVDGNKVSN KVKLRPGKYY LLVYKYSGSG NYELRVNK
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
912288
Matsushita O.,Jung C.-M.,Katayama S.,Minami J.,Takahashi Y.,Okabe A.
Gene duplication and multiplicity of collagenases in Clostridium histolyticum.
J. Bacteriol.
181
923-933
1999
912290
Bond M.D.,Van Wart H.E.
Characterization of the individual collagenases from Clostridium histolyticum.
Biochemistry
23
3085-3091
1984
912291
Mookhtiar K.A.,Steinbrink D.R.,Van Wart H.E.
Mode of hydrolysis of collagen-like peptides by class I and class II Clostridium histolyticum collagenases: evidence for both endopeptidase and tripeptidylcarboxypeptidase activities.
Biochemistry
24
6527-6533
1985
912292
Gelbard M.K.,James K.,Riach P.,Dorey F.
Collagenase versus placebo in the treatment of Peyronie's disease: a double-blind study.
J. Urol.
149
56-58
1993
912293
Fecteau K.A.,Haffner J.C.,Eiler H.
The potential of collagenase as a new therapy for separation of human retained placenta: hydrolytic potency on human, equine and bovine placentae.
Placenta
19
379-383
1998
912294
Badalamente M.A.,Hurst L.C.
Enzyme injection as nonsurgical treatment of Dupuytren's disease.
J. Hand Surg. Am.
25
629-636
2000
912295
Toyoshima T.,Matsushita O.,Minami J.,Nishi N.,Okabe A.,Itano T.
Collagen-binding domain of a Clostridium histolyticum collagenase exhibits a broad substrate spectrum both in vitro and in vivo.
Connect. Tissue Res.
42
281-290
2001
912296
Matsushita O.,Koide T.,Kobayashi R.,Nagata K.,Okabe A.
Substrate recognition by the collagen-binding domain of Clostridium histolyticum class I collagenase.
J. Biol. Chem.
276
8761-8770
2001
912297
McCarthy R.C.,Spurlin B.,Wright M.J.,Breite A.G.,Sturdevant L.K.,Dwulet C.S.,Dwulet F.E.
Development and characterization of a collagen degradation assay to assess purified collagenase used in islet isolation.
Transplant. Proc.
40
339-342
2008
912298
Eckhard U.,Schoenauer E.,Ducka P.,Briza P.,Nuess D.,Brandstetter H.
Biochemical characterization of the catalytic domains of three different Clostridial collagenases.
Biol. Chem.
390
11-18
2009
912299
Philominathan S.T.,Koide T.,Hamada K.,Yasui H.,Seifert S.,Matsushita O.,Sakon J.
Unidirectional binding of clostridial collagenase to triple helical substrates.
J. Biol. Chem.
284
10868-10876
2009
912300
Shi L.,Carson D.
Collagenase Santyl ointment: a selective agent for wound debridement.
J. Wound Ostomy Continence Nurs.
36
0-0
2009
912301
Hurst L.C.,Badalamente M.A.,Hentz V.R.,Hotchkiss R.N.,Kaplan F.T.,Meals R.A.,Smith T.M.,Rodzvilla J.
Injectable collagenase clostridium histolyticum for Dupuytren's contracture.
N. Engl. J. Med.
361
968-979
2009
912302
Breite A.G.,McCarthy R.C.,Dwulet F.E.
Characterization and functional assessment of Clostridium histolyticum class I (C1) collagenases and the synergistic degradation of native collagen in enzyme mixtures containing class II (C2) collagenase.
Transplant. Proc.
43
3171-3175
2011
912303
Philominathan S.T.,Koide T.,Matsushita O.,Sakon J.
Bacterial collagen-binding domain targets undertwisted regions of collagen.
Protein Sci.
21
1554-1565
2012
912304
Eckhard U.,Huesgen P.F.,Brandstetter H.,Overall C.M.
Proteomic protease specificity profiling of clostridial collagenases reveals their intrinsic nature as dedicated degraders of collagen.
J. Proteomics
100
102-114
2014
912305
Lipshultz L.I.,Goldstein I.,Seftel A.D.,Kaufman G.J.,Smith T.M.,Tursi J.P.,Burnett A.L.
Clinical efficacy of collagenase Clostridium histolyticum in the treatment of Peyronie's disease by subgroup: results from two large, double-blind, randomized, placebo-controlled, phase III studies.
BJU Int.
116
650-656
2015
912306
Schoenauer E.,Kany A.M.,Haupenthal J.,Huesecken K.,Hoppe I.J.,Voos K.,Yahiaoui S.,Elsaesser B.,Ducho C.,Brandstetter H.,Hartmann R.W.
Discovery of a potent inhibitor class with high selectivity toward clostridial collagenases.
J. Am. Chem. Soc.
139
12696-12703
2017
912307
Wilson J.J.,Matsushita O.,Okabe A.,Sakon J.
A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation.
EMBO J.
22
1743-1752
2003
912309
Eckhard U.,Brandstetter H.
Polycystic kidney disease-like domains of clostridial collagenases and their role in collagen recruitment.
Biol. Chem.
392
1039-1045
2011
912310
Eckhard U.,Schonauer E.,Nuss D.,Brandstetter H.
Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis.
Nat. Struct. Mol. Biol.
18
1109-1114
2011
912311
Bauer R.,Wilson J.J.,Philominathan S.T.,Davis D.,Matsushita O.,Sakon J.
Structural comparison of ColH and ColG collagen-binding domains from Clostridium histolyticum.
J. Bacteriol.
195
318-327
2013
912312
Eckhard U.,Schonauer E.,Brandstetter H.
Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T.
J. Biol. Chem.
288
20184-20194
2013
912313
Bauer R.,Janowska K.,Taylor K.,Jordan B.,Gann S.,Janowski T.,Latimer E.C.,Matsushita O.,Sakon J.
Structures of three polycystic kidney disease-like domains from Clostridium histolyticum collagenases ColG and ColH.
Acta Crystallogr. D
71
565-577
2015