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Items: 8

1.

Neurolysin/Thimet oligopeptidase, N-terminal domain

Thimet oligopeptidase and neurolysin are closely related zinc-dependent metallopeptidases that metabolize small bioactive peptides. They cleave many substrates at the same sites, but they recognise different positions on others. This entry represents the up-down alpha bundle domain found at the N terminus of these and related M3 peptidases. Paper describing PDB structure 1i1i. [1]. 11248043. Structure of neurolysin reveals a deep channel that limits. substrate access.. Brown CK, Madauss K, Lian W, Beck MR, Tolbert WD, Rodgers DW;. Proc Natl Acad Sci U S A. 2001;98:3127-3132.. Paper describing PDB structure 1s4b. [2]. 14998993. Crystal structure of human thimet oligopeptidase provides. insight into substrate recognition, regulation, and. localization.. Ray K, Hines CS, Coll-Rodriguez J, Rodgers DW;. J Biol Chem. 2004;279:20480-20489.. Paper describing PDB structure 1y79. [3]. 15876371. Crystal structure of the E. coli dipeptidyl carboxypeptidase. Dcp: further indication of a ligand-dependent hinge movement. mechanism.. Comellas-Bigler M, Lang R, Bode W, Maskos K;. J Mol Biol. 2005;349:99-112.. Paper describing PDB structure 2o36. [4]. 17251185. Swapping the substrate specificities of the neuropeptidases. neurolysin and thimet oligopeptidase.. Lim EJ, Sampath S, Coll-Rodriguez J, Schmidt J, Ray K, Rodgers. DW;. J Biol Chem. 2007;282:9722-9732.. Paper describing PDB structure 4fxy. [5]. 25378390. Allosteric inhibition of the neuropeptidase neurolysin.. Hines CS, Ray K, Schmidt JJ, Xiong F, Feenstra RW, Pras-Raves M,. de Moes JP, Lange JH, Melikishvili M, Fried MG, Mortenson P,. Charlton M, Patel Y, Courtney SM, Kruse CG, Rod. TRUNCATED at 1650 bytes (from Pfam)

Date:
2024-08-14
Family Accession:
NF040252.4
Method:
HMM
2.

M3 family metallopeptidase

This is the Thimet oligopeptidase family, large family of mammalian and bacterial oligopeptidases that cleave medium sized peptides. The group also contains mitochondrial intermediate peptidase which is encoded by nuclear DNA but functions within the mitochondria to remove the leader sequence. [1]. 7674922. Evolutionary families of metallopeptidases.. Rawlings ND, Barrett AJ;. Meth Enzymol 1995;248:183-228. (from Pfam)

GO Terms:
Molecular Function:
metalloendopeptidase activity (GO:0004222)
Biological Process:
proteolysis (GO:0006508)
Date:
2024-08-14
Family Accession:
NF013591.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

M3 family metallopeptidase

M3 family metallopeptidase with varied activities, and contains the HEXXH motif that forms the active site in conjunction with a C-terminally-located Glu residue

Date:
2019-02-20
Family Accession:
11485081
Method:
Sparcle
8.

oligopeptidase A

Gene:
prlC
GO Terms:
Molecular Function:
metalloendopeptidase activity (GO:0004222)
Biological Process:
proteolysis (GO:0006508)
Date:
2021-08-04
Family Accession:
NF008159.0
Method:
HMM
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