Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.4.24.3 - microbial collagenase and Organism(s) Clostridium tetani and UniProt Accession Q899Y1

for references in articles please use BRENDA:EC3.4.24.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.3 microbial collagenase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Clostridium tetani
UNIPROT: Q899Y1 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Clostridium tetani
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
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'
Synonyms
bacterial collagenase, collagenase clostridium histolyticum, type i collagenase, collagenase i, clostridial collagenase, clostridium histolyticum collagenase, type ii collagenase, clostridiopeptidase a, collagenase g, collagenase h, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
120 kDa collagenase
-
-
-
-
Achromobacter iophagus collagenase
-
-
-
-
aspergillopeptidase C
-
-
-
-
azocollase
-
-
-
-
clostridiopeptidase A
-
-
-
-
clostridiopeptidase I
-
-
-
-
clostridiopeptidase II
-
-
-
-
Clostridium histolyticum collagenase
-
-
-
-
collagen peptidase
-
-
-
-
collagen protease
-
-
-
-
collagenase A
-
-
-
-
collagenase I
-
-
-
-
collagenase MMP-1
-
-
-
-
collagenase T
-
-
kollaza
-
-
-
-
matirx metalloproteinase-18
-
-
-
-
matrix metalloproteinase-1
-
-
-
-
metallocollagenase
-
-
-
-
metalloproteinase-1
-
-
-
-
MMP-1
-
-
-
-
nucleolysin
-
-
-
-
peptidase, clostridio-, A
-
-
-
-
proteinase, Clostridium histolyticum, A
-
-
-
-
soycollagestin
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9001-12-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
furylacryloyl-Leu-Gly-Pro-Ala + H2O
furylacryloyl-Leu + Gly-Pro-Ala
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zinc
-
expression of a truncated construct Y53-A506 which stops shortly after the third zinc binding residue and consitstent with the prediction of a minimal catalytic domain. The construct shows no catalytic activity at all, despite containing all zinc binding residues including the catalytic glutamate that is supposed to act as general base
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
-
The half maximal inhibitory concentrations of the catalytic domains for 1,10-phenanthroline are significantly decreased in the presence of the N-terminal His6-tag
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.97 - 1.24
furylacryloyl-Leu-Gly-Pro-Ala
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.65 - 7.24
furylacryloyl-Leu-Gly-Pro-Ala
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04 - 0.15
1,10-phenanthroline
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform ColT
UniProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the peptidase domains of ColT in the presence and absence of the peptidic inhibitor isoamylphosphonyl-Gly-Pro-Ala bound to the active site. Comparison of isoforms ColH, ColT and ColG reveals differences in domain breathing motions and regulatory elements. Calcium and zinc are required for full peptidolytic activity
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
addition of an N-terminal His-tag. The Michaelis-Menten constant of ColT increases by approximately 60%. Expression of a truncated construct Y53-A506 which stops shortly after the third zinc binding residue and consitstent with the prediction of a minimal catalytic domain. The construct shows no catalytic activity at all, despite containing all zinc binding residues including the catalytic glutamate that is supposed to act as general base
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Hathewaya histolytica, Clostridium tetani
Manually annotated by BRENDA team
Eckhard, U.; Schoenauer, 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
Hathewaya histolytica (Q46085), Hathewaya histolytica (Q9X721), Clostridium tetani (Q899Y1), Clostridium tetani E88 (Q899Y1)
Manually annotated by BRENDA team