F5135

N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala

Name: N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala
Brand: SIGMA

collagenase substrate, chromogenic

Synonyme(s) :

FALGPA, N-[3-(2-Furyl)acryloyl]-L-leucyl-glycyl-L-prolyl-L-alanine

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About This Item

Formule empirique (notation de Hill) :

C₂₃H₃₂N₄O₇

Numéro CAS:

78832-65-2

Poids moléculaire :

476.52

UNSPSC Code:

12352202

PubChem Substance ID:

329799652

NACRES:

NA.32

MDL number:

MFCD00133552

Nom du produit

N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala,

SMILES string

CC(C)C[C@H](NC(=O)\C=C\c1ccco1)C(=O)NCC(=O)N2CCC[C@H]2C(=O)N[C@@H](C)C(O)=O

InChI

1S/C23H32N4O7/c1-14(2)12-17(26-19(28)9-8-16-6-5-11-34-16)21(30)24-13-20(29)27-10-4-7-18(27)22(31)25-15(3)23(32)33/h5-6,8-9,11,14-15,17-18H,4,7,10,12-13H2,1-3H3,(H,24,30)(H,25,31)(H,26,28)(H,32,33)/b9-8+/t15-,17-,18-/m0/s1

InChI key

ZLFQNOJSYZSINX-PVJKAEHXSA-N

UniProt accession no.

Q02111

storage temp.

−20°C

Quality Level

200

Gene Information

mouse ... Prkcq(18761)

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Application

N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala has been used for use in FALGPA assay performed using GBS (Group B Streptococci) USF704.

Biochem/physiol Actions

N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala or FALGPA is hydrolyzed by collagenases and the optimum pH for hydrolysis is 7.4.

General description

N-[3-(2-Furyl)acryloyl]-Leu-Gly-Pro-Ala or FALGPA is a synthetic substance which resemble the primary structure of collagen, and is hydrolyzed by all known collagenases.

Substrate for collagenase.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Classe de stockage

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Consulter la Bibliothèque de documents

Purification and substrate specificity of an endopeptidase from the human oral spirochete Treponema denticola ATCC 35405, active on furylacryloyl-Leu-Gly-Pro-Ala and bradykinin.

K K Mäkinen et al.

The Journal of biological chemistry, 267(20), 14285-14293 (1992-07-15)

An endopeptidase was purified to homogeneity from the cell extracts of Treponema denticola ATCC 35405 (a human oral spirochete) by a procedure that comprised dialysis, anion exchange fast protein liquid chromatography (FPLC), hydroxylapatite FPLC, immobilized metal affinity FPLC, FPLC chromatofocusing

Characterization of PepB, a group B streptococcal oligopeptidase.

B Lin et al.

Infection and immunity, 64(8), 3401-3406 (1996-08-01)

Group B streptococci were recently reported to possess a cell-associated collagenase. Although the enzyme hydrolyzed the synthetic collagen-like substrate N-(3-[2-furyl]acryloyl)-Leu-Gly-Pro-Ala, we found that neither the highly purified enzyme nor crude group B streptococcal cell lysate solubilized a film of reconstituted

Comparative studies on the activities of collagenases from Grimontia hollisae and Clostridium hystoliticum in the hydrolysis of synthetic substrates.

Teisuke Takita et al.

Journal of biochemistry, 163(5), 425-431 (2018-02-15)

The collagenase produced by a gram-negative bacterium Grimontia hollisae strain 1706B (Ghcol) degrades collagen more efficiently than that produced by a gram-positive bacterium Clostridium histolyticum (Chcol), which is currently the most widely used collagenase in industry [Teramura et al. (Cloning

Biochemical comparison of proteolytic enzymes present in rough- and smooth-surfaced capnocytophagas isolated from the subgingival plaque of periodontitis patients.

E Söderling et al.

Journal of periodontal research, 26(1), 17-23 (1991-01-01)

Four rough-surfaced (R) and three smooth-surfaced (S) clinical isolates of Capnocytophaga obtained from the subgingival plaque of periodontitis patients were studied for their peptidase and protease profiles. The results were compared with those obtained with C. gingivalis (which has a

Inhibition of collagenase by Cr(III): its relevance to stabilization of collagen.

R Gayatri et al.

Biochimica et biophysica acta, 1524(2-3), 228-237 (2000-12-13)

Bacterial collagenase has now been reacted with a select series of Cr(III) complexes and modifications in the activity of chromium-modified collagenase has been deduced from the extent of hydrolysis of (2-furanacryloyl-L-leucyl-glycyl-L-prolyl-L-alanine), FALGPA. A homologous series of Cr(III) complexes with dimeric

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