MG_020_MONOMER – proline iminopeptidase

Name
WID MG_020_MONOMER View in model
Name proline iminopeptidase View in model
 
Genetics
Gene MG_020 View in model
 
Structure
Sequence
1
51
101
151
201
251
301
MNTKLNVKGYLNVGDNHQLYYWTQGNPNGKPVLYIHGGPGSGTDEGCLKY
FDLETTWIILLDQRGCGKSKTNDIFYENNTDKLVSDFEILRQKLNIKNWT
LFGGSWGSALALVYAIKHPQVVDKIFLRALFLAREKDWSEALMGLGKMFY
PYEHQRFMDSIPKAYQNSYEQIVNYCYDQFQNGDESTKEKLAKAWVDWES
TLLSPINKIHSTATDFKLVEKLALLECHYAVNKSFLDENFILDNISVLKN
KSIYLAHGRFDLICPLYQPLALKQAFPELQLYVTNNAGHSGSDANNLATI
KHLLKTYL*
50
100
150
200
250
300
309
View in model
Is N‑terminal methionine cleaved
No
View in model
Prosthetic groups View in model
Empirical formula (pH 7.5) H2456C1613N413O461S9
Molecular weight (pH 7.5; Da) 35297.74 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
65945
Instability index 23.78
Is stable True
Aliphatic index 89.97
GRAVY (25C, pH 7.0) -0.329
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200 View in model
 
Synthesis
Localization c View in model
 
Comments
Comments Functional Macromolecule Functional as monomer [PUB_0037]. Coenzymes Monomer interacts with MN with unknown stoichiometry as prosthetic group [33].
References
  1. Yoshimoto T, Kabashima T, Uchikawa K, Inoue T, Tanaka N, Nakamura KT, Tsuru M, Ito K. Crystal structure of prolyl aminopeptidase from Serratia marcescens. J Biochem 126, 559-65 (1999). WholeCell: PUB_0037, PubMed: 10467172

 
Metadata
Created 2012-10-01 15:07:44
Last updated 2012-10-01 15:14:21