KEGG   ENZYME: 3.4.24.3Help
Entry
EC 3.4.24.3                 Enzyme                                 

Name
microbial collagenase;
Clostridium histolyticum collagenase;
clostridiopeptidase A;
collagenase A;
collagenase I;
Achromobacter iophagus collagenase;
collagenase;
aspergillopeptidase C;
nucleolysin;
azocollase;
metallocollagenase;
soycollagestin;
Clostridium histolyticum proteinase A;
clostridiopeptidase II;
MMP-8;
clostridiopeptidase I;
collagen peptidase;
collagen protease;
collagenase MMP-1;
metalloproteinase-1;
kollaza;
matrix metalloproteinase-1;
MMP-1;
matrix metalloproteinase-8;
matirx metalloproteinase-18;
interstitial collagenase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Metalloendopeptidases
BRITE hierarchy
Reaction(IUBMB)
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'
Comment
Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum. Class I has forms alpha (68 kDa), beta (115 kDa) and gamma (79 kDa); class II has delta (100 kDa), epsilon (110 kDa) and zeta (125 kDa). The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary. The enzymes also act as peptidyl-tripeptidases. Variants of the enzyme have been purified from Bacillus cereus [10], Empedobacter collagenolyticum [4], Pseudomonas marinoglutinosa [1], and species of Vibrio, Vibrio B-30 (ATCC 21250) [2] and V. alginolyticus (previously Achromobacter iophagus) [3,8]. Also known from Streptomyces sp. [9]. The Vibrio enzyme is the type example of peptidase family M9.
History
EC 3.4.24.3 created 1961 as EC 3.4.4.19, transferred 1972 to EC 3.4.24.3 (EC 3.4.24.8 created 1978, incorporated 1992, EC 3.4.99.5 created 1972, incorporated 1978)
Orthology
K01387  
microbial collagenase
Genes
SGL: 
VCH: 
VCE: 
VCJ: 
VCO: 
VCM: 
VCI: 
VCL: 
VCQ: 
VVU: 
VVY: 
VVM: 
VVL: 
VPA: 
VPB: 
VPK: 
VPF: 
VPH: 
VHA: 
VCA: 
VAG: 
VEX: 
VNI: 
VAN: 
LAG: 
VCY: 
VTU: 
SON: 
SAZ: 
SBL: 
SBM: 
SBN: 
SBP: 
SBT: 
SBS: 
SBB: 
SLO: 
SSE: 
SPL: 
SHL: 
SWD: 
SWP: 
SVO: 
CPS: 
FBL: 
HCH: 
SAGA: 
CVI: 
BMA: 
BML: 
BMN: 
BMAL: 
BPS: 
BPM: 
BPL: 
BPD: 
BPSE: 
BPSM: 
BPSU: 
BPSD: 
BPZ: 
BPQ: 
BPK: 
BPSH: 
BTE: 
BTQ: 
BTJ: 
BTZ: 
BTD: 
BTV: 
BTHE: 
BTHM: 
BOK: 
BUT: 
BUR: 
MXA: 
MSD: 
BAN: 
BAR: 
BAT: 
BAH: 
BAI: 
BAX: 
BANT: 
BANR: 
BANS: 
BANH: 
BAL: 
BCE: 
BCA: 
BCZ: 
BCZK0466(colA) BCZK3238(colA) pE33L466_0145(colA)
BCR: 
BCB: 
BCU: 
BCG: 
BCQ: 
BCQ_0620(colA) BCQ_3316(colA)
BCX: 
BNC: 
BCF: 
BCER: 
BCEF: 
BCY: 
BTK: 
BTL: 
BTB: 
BTT: 
BTHR: 
BTC: 
BTF: 
BTM: 
BTG: 
BTB_c05690(colA1) BTB_c31330(colA2) BTB_c36010(colA3)
BTI: 
BTN: 
BTHT: 
BTHU: 
BWE: 
BTY: 
BMYC: 
LSP: 
BBE: 
PLV: 
CPE: 
CPE0173(colA)
CPF: 
CPF_0166(colA)
CPR: 
CPR_0162(colA)
CTC: 
pE88_34(colT)
CTET: 
CNO: 
CBO: 
CBO1620(colA)
CBA: 
CBH: 
CBY: 
CLM_1861(colG)
CBL: 
CBK: 
CBB: 
CBI: 
CLJ_B1730(colG)
CBN: 
CBT: 
CBF: 
CBJ: 
SCO: 
SCO5912(SC10A5.17)
SGR: 
SVL: 
SCT: 
SCY: 
SVE: 
SFI: 
SCI: 
SRC: 
SLV: 
SGU: 
KSK: 
ARR: 
SRO: 
SEN: 
SESP: 
MIL: 
CAI: 
SNA: 
LIL: 
LIE: 
LIC: 
LBJ: 
LBJ_0742(colA)
LBL: 
LBL_2336(colA)
 » show all
Taxonomy
Reference
1
  Authors
Hanada, K., Mizutani, T., Yamagishi, M., Tsuji, H., Misaki, T. Sawada, J.
  Title
The isolation of collagenase and its enzymological and physico-chemical properties.
  Journal
Agric. Biol. Chem. 37 (1973) 1771-1781.
Reference
2  [PMID:210785]
  Authors
Merkel JR, Dreisbach JH.
  Title
Purification and characterization of a marine bacterial collagenase.
  Journal
Biochemistry. 17 (1978) 2857-63.
Reference
3  [PMID:6250633]
  Authors
Heindl MC, Fermandjian S, Keil B.
  Title
Circular dichroism comparative studies of two bacterial collagenases and thermolysin.
  Journal
Biochim. Biophys. Acta. 624 (1980) 51-9.
Reference
4  [PMID:6530724]
  Authors
Waid DD, Warren RJ, Pence DB.
  Title
Elaeophora schneideri Wehr and Dickmans, 1935 in white-tailed deer from the Edwards Plateau of Texas.
  Journal
J. Wildl. Dis. 20 (1984) 342-5.
Reference
5  [PMID:6087888]
  Authors
Bond MD, Van Wart HE.
  Title
Characterization of the individual collagenases from Clostridium histolyticum.
  Journal
Biochemistry. 23 (1984) 3085-91.
Reference
6  [PMID:6087889]
  Authors
Bond MD, Van Wart HE.
  Title
Relationship between the individual collagenases of Clostridium histolyticum: evidence for evolution by gene duplication.
  Journal
Biochemistry. 23 (1984) 3092-9.
Reference
7  [PMID:3002445]
  Authors
Van Wart HE, Steinbrink DR.
  Title
Complementary substrate specificities of class I and class II collagenases from Clostridium histolyticum.
  Journal
Biochemistry. 24 (1985) 6520-6.
Reference
8
  Authors
Tong, N.T., Tsugita, A. and Keil-Dlouha, V.
  Title
Purification and characterization of two high-molecular-mass forms of Achromobacter collagenase.
  Journal
Biochim. Biophys. Acta 874 (1986) 296-304.
Reference
9  [PMID:2822678]
  Authors
Endo A, Murakawa S, Shimizu H, Shiraishi Y.
  Title
Purification and properties of collagenase from a Streptomyces species.
  Journal
J. Biochem. (Tokyo). 102 (1987) 163-70.
Reference
10 [PMID:3040751]
  Authors
Makinen KK, Makinen PL.
  Title
Purification and properties of an extracellular collagenolytic protease produced by the human oral bacterium Bacillus cereus (strain Soc 67).
  Journal
J. Biol. Chem. 262 (1987) 12488-95.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9001-12-1

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