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: SG1493
LAB: LA76x_0536 LA76x_4670
LAQ: GLA29479_2609 GLA29479_4489
LCP: LC55x_0373
LGU: LG3211_0395
LEZ: GLE_0220
LEM: LEN_4723
VCH: VC1650
VCF: IR04_13470
VCS: MS6_1430
VCI: O3Y_08015
VCM: VCM66_1589(vcc)
VCX: VAA049_1153(prt)
VCZ: VAB027_2297(prt)
VVU: VV2_1146
VVY: VVA1672
VNI: VIBNI_B0933(prt)
VAN: VAA_02998
VAU: VANGNB10_cII0222(expA)
SON: SO_0639
SBL: Sbal_3732
PSPO: PSPO_a0484(colA) PSPO_a1890(colA) PSPO_a2170(colA)
PTU: PTUN_a0184(colA) PTUN_a1257(colA)
MVS: MVIS_3532
HCH: HCH_05788
BMA: BMAA0694
BMAL: DM55_4743
BMAE: DM78_3247
BMAQ: DM76_3697
BMAI: DM57_12100
BMAF: DM51_4400
BMAZ: BM44_4733
BPS: BPSS0666
BTQ: BTQ_4865
BTJ: BTJ_3490
BTZ: BTL_4339
BTD: BTI_5644
BTV: BTHA_3618
BTHE: BTN_3990
BTHM: BTRA_4103
BTHA: DR62_4026
BTHL: BG87_4321
BOK: DM82_4997
BOC: BG90_5598
BCON: NL30_31580
BUB: BW23_582
BSTG: WT74_18870
BUL: BW21_5331
CARE: LT85_1390
MXA: MXAN_6205
BCZ: BCE33L0466(colA) BCE33L3238(colA) pE33L466_0145(colA)
BCQ: BCQ_0620(colA) BCQ_3316(colA)
BAL: BACI_c05630(colC) BACI_c34720(colA2)
BTK: BT9727_0466(colA) BT9727_3286(colA)
BTL: BALH_0495(colA) BALH_3172
BTG: BTB_c05690(colA1) BTB_c31330(colA2) BTB_c36010(colA3)
BWW: bwei_1412(colA2) bwei_2005(colA5) bwei_5050(colA4) bwei_5337(colA1)
LSP: Bsph_2533
BBE: BBR47_37890(colA) BBR47_42950(colA)
PLV: ERIC2_c40370(colA)
CPE: CPE0173
CPF: CPF_0166(colA)
CPR: CPR_0162(colA)
CTC: CTC_p33(colT)
CTET: BN906_02951(colT)
CBO: CBO1620(colA)
CBA: CLB_1638(colG)
CBH: CLC_1647
CBY: CLM_1861(colG)
CBL: CLK_1084(colG)
CBK: CLL_A1484(colG)
CBB: CLD_2936(colG)
CBI: CLJ_B1730(colG)
CBN: CbC4_0444
CBT: CLH_1400(colG)
CBF: CLI_1698
CLD: CLSPO_c16750(colA)
SCO: SCO5912(SC10A5.17)
SGR: SGR_1615
SGB: WQO_27370
SVE: SVEN_7132
SFI: SFUL_5845
STRE: GZL_00476
SLD: T261_0204
STRM: M444_26285
SPRI: SPRI_1204
SLAU: SLA_7008
SALF: SMD44_06979(colA)
SALJ: SMD11_0557(colA)
SRO: Sros_3516
SEN: SACE_3082
SESP: BN6_23720
ALL: CRK56022
MIL: ML5_4364
SNA: Snas_2903
LIL: LA_0872
LIE: LIF_A0713
LIC: LIC_12760
LIS: LIL_12850
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 37:1771-1781 (1973)
Reference
2  [PMID:210785]
  Authors
Merkel JR, Dreisbach JH.
  Title
Purification and characterization of a marine bacterial collagenase.
  Journal
Biochemistry 17:2857-63 (1978)
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 624:51-9 (1980)
DOI:10.1016/0005-2795(80)90224-X
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 20:342-5 (1984)
Reference
5  [PMID:6087888]
  Authors
Bond MD, Van Wart HE.
  Title
Characterization of the individual collagenases from Clostridium histolyticum.
  Journal
Biochemistry 23:3085-91 (1984)
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 23:3092-9 (1984)
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 24:6520-6 (1985)
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 874:296-304 (1986)
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) 102:163-70 (1987)
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 262:12488-95 (1987)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.24.3
IUBMB Enzyme Nomenclature: 3.4.24.3
ExPASy - ENZYME nomenclature database: 3.4.24.3
BRENDA, the Enzyme Database: 3.4.24.3
CAS: 9001-12-1

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