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Literature summary for 3.4.24.7 extracted from

  • Stawikowski, M.J.; Stawikowska, R.; Fields, G.B.
    Collagenolytic matrix metalloproteinase activities toward peptomeric triple-helical substrates (2015), Biochemistry, 54, 3110-3121 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.7

Protein Variants

Protein Variants Comment Organism
additional information incorporation of peptoid residues into collagen model triple-helical peptides and examination of MMP activities toward the peptomeric chimeras Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
EDTA complete inhibition Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic analysis, Michaelis-Menten kinetic model Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required Homo sapiens
Zn2+ zinc metalloproteinase Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Collagen type III + H2O Homo sapiens
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P03956
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(GP4Hyp)4-GPQGIAGQRGVVGL4Hyp(GP4Hyp)4-NH2 + H2O alpha1(I)772-786 THP Homo sapiens (GP4Hyp)4-GPQG + IAGQRGVVGL4Hyp(GP4Hyp)4-NH2
-
 ?
(GP4Hyp)4GPQ-Sar-IAGQRGVVG-Nle-GL4Hyp(GP4Hyp)4-NH2 + H2O
-
 Homo sapiens (GP4Hyp)4GPQ-Sar + IAGQRGVVG-Nle-GL4Hyp(GP4Hyp)4-NH2
-
 ?
(GP4Hyp)4GPQ-Sar-IAGQRGVVGL4Hyp(GP4Hyp)4-NH2 + H2O
-
 Homo sapiens (GP4Hyp)4GPQ-Sar + IAGQRGVVGL4Hyp(GP4Hyp)4-NH2
-
 ?
(GP4Hyp)4GPQGIAGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2 + H2O the substrate is hydrolyzed at the Gly775-Ile776 bond by the enzyme Homo sapiens (GP4Hyp)4GPQG + IAGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2
-
 ?
Collagen type III + H2O
-
 Homo sapiens ?
-
 ?
additional information several different peptoid residues are incorporated into triple helical substrates at subsites P3, P1, P1', and P10' individually or in combination, and the effects of the peptoid residues are evaluated on the activities of full-length MMP-1 and other MMPs, collagenolytic matrix metalloproteinase activities toward peptomeric triple-helical substrates, overview. Most peptomers show little discrimination between MMPs. A peptomer containing N-methyl Gly (sarcosine) in the P1' subsite and N-isobutyl Gly (Nle) in the P10' subsite is not hydrolysed by MMP-1. Also no activity with (GP4Hyp)4-GPQG-Sar-AGQRGVVGL4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GPQG-Sar-AGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4G-Sar-QGIAGQRGVVGL4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GPQGWAGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4-GPQG-NIle-AGQRGVVGL4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GPQG-Sar-AGQRGVVG-Nle-4Hyp(GP4Hyp)4-NH2, (GP4Hyp)4GP-Lys(Mca)-G-Sar-AGQRGV-Lys(Dnp)-GNle-4Hyp(GP4Hyp)4-NH2 and Ac-(GP4Hyp)4-GP-Lys(Mca)-G-Sar-AGQRGV-Lys(Dnp)G-Nle-4Hyp(GP4Hyp)4-NH2, 4Hyp is hydroxyproline. The P10' subsite is important for collagenous substrate interaction with MMP-1, and this interaction occurs via the HPX domain. Molecular dynamics (MD) simulations, model of MMP-1 with the alpha1(I)772-786 THP, overview Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
collagenolytic matrix metalloproteinase
-
 Homo sapiens
MMP-1
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Homo sapiens

General Information

General Information Comment Organism
additional information although collagenolytic matrix metalloproteinases (MMPs) possess common domain organizations, there are subtle differences in their processing of collagenous triple-helical substrates Homo sapiens