protein

E. Coli Recombinant SlyD

MBS845366

0.1 mg

390 USD

Recombinant Protein

E. Coli Recombinant SlyD

[SlyD]

[FKBP-type peptidyl-prolyl cis-trans isomerase.; E. Coli Recombinant SlyD]

[FKBP-type peptidyl prolyl cis-trans isomerase (rotamase); FKBP-type peptidyl-prolyl cis-trans isomerase SlyD; FKBP-type peptidyl prolyl cis-trans isomerase (rotamase); Histidine-rich protein; Metallochaperone SlyD; Rotamase; Sensitivity to lysis protein D; WHP]

[SLYD]

[slyD; slyD; ECK3336; JW3311; PPIase]

SLYD_ECOLI

196

MKVAKDLVVS LAYQVRTEDG VLVDESPVSA PLDYLHGHGS LISGLETALE GHEVGDKFDV AVGANDAYGQ YDENLVQRVP KDVFMGVDEL QVGMRFLAET DQGPVPVEIT AVEDDHVVVD GNHMLAGQNL KFNVEVVAIR EATEEELAHG HVHGAHDHHH DHDHDGCCGG HGHDHGHEHG GEGCCGGKGN GGCGCH

>=95% by SDS-PAGE

1 mg/ml solution in 20 mM Tris-HCl (pH 7.5).

Can be stored at 4°C short term (1-2 weeks). For long term storage, aliquot and store at -20°C or -70°C. Avoid repeated freezing and thawing cycles.

SDS-PAGE

Testing Data

Source: E.coli

Biological activity: Specific activity is >220 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1 umole of Suc-AAFP-pNA per minute at 25°C in Tris HCI pH 8.0 using chymotypsin.

Proteins and Enzymes; Proteins and Enzymes (A-Z)

Background: SlyD is a putative folding helper protein from the Escherichia coli cytosol, which consists of an N-terminal prolyl isomerase domain of the FKBP type and a presumably unstructured C-terminal tail. It is involved in the biosynthesis of the metal cluster in the [NiFe]-hydrogenase enzymes, and exhibits several activities including that of a peptidyl-prolyl isomerase.

16131228

NP_417808.1

NC_000913.3

P0A9K9

21 kDa (196 aa, 1-196 aa)

HypB requires binding of SlyD for hydrogenase activity as SlyD helps facilitate nickel insertion. [More information is available at EcoGene: EG11663]. SlyD is a peptidyl prolyl cis/trans-isomerase (PPIase) and chaperone. [More information is available at EcoCyc: EG11663].

Folding helper with both chaperone and peptidyl-prolyl cis-trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa-Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction. SlyD could be involved in Tat-dependent translocation, by binding to the Tat-type signal of folded proteins. The PPIase substrate specificity, carried out with synthetic peptides of the 'suc-Ala-Xaa-Pro-Phe-4NA' type (where Xaa is the AA tested), was found to be Phe > Ala > Leu.

0.1 mg

390 USD