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3.4.24.85: S2P endopeptidase

This is an abbreviated version!
For detailed information about S2P endopeptidase, go to the full flat file.

Word Map on EC 3.4.24.85

Reaction

Cleaves several transcription factors that are type-2 transmembrane proteins within membrane-spanning domains. Known substrates include sterol regulatory element-binding protein (SREBP) -1, SREBP-2 and forms of the transcriptional activator ATF6. SREBP-2 is cleaved at the site DRSR_ILL_483-/-CVLTFLCLSFNPLTSLLQWGGA, in which the membrane-spanning segment is underlined. The residues NP (bold), 11 residues distal to the site of cleavage in the membrane-spanning domain, are important for cleavage by S2P endopeptidase. Replacement of either of these residues does not prevent cleavage, but there is no cleavage if both of these residues are replaced. =

Synonyms

EcfE, Eep, HurP, I-CLiP, intramembrane-cleaving protease, MEROPS:M50, MmpA, MucP, proteinase, sterol regulatory element-binding protein, RasP, RseP, Rv2869c, S2P, S2P protease, site-1 protease, site-2 metalloprotease, site-2 protease, site-2-protease, sll0528, Slr0643, Slr1821, SPOIVFB, Sre2, SREBP cleavage activity, SREBP cysteine proteinase, SREBP proteinase, SREBP-1 proteinase, SREBP-2 proteinase, sterol regulatory element binding protein, sterol regulatory element binding protein-2 proteinase, sterol regulatory element-binding proteinase, sterol-regulated protease, Stp1, YaeL, YluC

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.24 Metalloendopeptidases
                3.4.24.85 S2P endopeptidase

Engineering

Engineering on EC 3.4.24.85 - S2P endopeptidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H22F
-
active site mutant
D402N
abolished activity
E23Q
abolished activity
H26F
abolished activity
D467N
mutation of aspartate abolish activity suggesting that is the third residue that coordinates the zinc active site of S2P
N337Q
mutation at glycosylation site N337 does not abolish activity
N508Q
mutation does not abolish activity
D148A
-
mutant exhibits markedly compromised protease activity
E55A
-
mutant exhibits markedly compromised protease activity
H54A
-
mutant exhibits markedly compromised protease activity
H54A/D148A
-
mutant exhibits markedly compromised protease activity
H58A
-
mutant exhibits markedly compromised protease activity
additional information