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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

Synonym(s):

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

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About This Item

Empirical Formula (Hill Notation):

C₂₃H₃₂N₄O₇

CAS Number:

78832-65-2

Molecular Weight:

476.52

MDL number:

MFCD00133552

UNSPSC Code:

12352202

PubChem Substance ID:

329799652

NACRES:

NA.32

product name

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

UniProt accession no.

Q02111

storage temp.

−20°C

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

Gene Information

mouse ... Prkcq(18761)

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Amino Acid Sequence

FA-Leu-Gly-Pro-Ala

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.

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.

Packaging

Bottomless glass bottle. Contents are inside inserted fused cone.

Substrates

Substrate for collagenase.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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

Expression and characterization of the prtV gene encoding a collagenase from Vibrio parahaemolyticus in Escherichia coli.

M S Yu et al.

Microbiology (Reading, England), 145 ( Pt 1), 143-150 (1999-04-17)

The prtV gene, encoding a collagenase of Vibrio parahaemolyticus, was expressed in Escherichia coli and purified by affinity chromatography. The transformant E. coli BL21(DE3)(pPRT2) secreted the recombinant PrtV, and the highest enzyme activity was detected in the culture supernatant after

An extracellular protease of Streptococcus gordonii hydrolyzes type IV collagen and collagen analogues.

Z E Juarez et al.

Infection and immunity, 67(1), 271-278 (1998-12-24)

Streptococcus gordonii is a frequent cause of infective bacterial endocarditis, but its mechanisms of virulence are not well defined. In this study, streptococcal proteases were recovered from spent chemically defined medium (CDM) and fractionated by ammonium sulfate precipitation and by

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Protocols

Enzymatic Assay of Collagenase (EC 3.4.24.3) using FALGPA (N-(3-[2-Furyl]acryloyl)-Leu-Gly-Pro-Ala)

To measure collagenase activity, N-(3-[2-Furyl]acryloyl)-Leu-Gly-Pro-Ala is used in a continuous spectrophotometric rate determination at 345 nm. Collagenase hydrolyzes collagen peptide bonds.

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