MG_324_MONOMER – aminopeptidase

Name
WID MG_324_MONOMER View in model
Name aminopeptidase View in model
 
Genetics
Gene MG_324 View in model
 
Structure
Sequence
1
51
101
151
201
251
301
351
MISELQQKITVLKDLLKTNKADAILIGSDQNRFWLTNFPSSAGWLIITSN
KAKLFIDGRYYEAARNFINPIVEVELFVSFKQVKAFCESNGINHLLIEGD
YLTFNYQDWIQAICKQYTVINAQEIRRVKLPSEIQAIEKAVDITRKVAVK
LKRFIKPKMTELFISQWITNELVKQGGAKNSFDPIVATGKNGANPHHKPT
KTIVKEGDFITCDFGTIYNGYCSDITRTFLVGKKPKSAKLLSAYKKVEEA
NLAGINAVNTTLTGSQVDKVCRDIIENSEFKDFFVHSTGHGVGIDIHEMP
NVSQSYNKLLCENGVVTIEPGIYIPNLGGIRIEDMVLVKKEKSVWLSKSI
PRAF*
50
100
150
200
250
300
350
355
View in model
Is N‑terminal methionine cleaved
No
View in model
Prosthetic groups View in model
Empirical formula (pH 7.5) H2874C1806N475O517S10
Molecular weight (pH 7.5; Da) 39833.55 View in model
Extinction coefficient 
(260 nm, 25C, pH 7.0)
43150
Instability index 26.59
Is stable True
Aliphatic index 96.37
GRAVY (25C, pH 7.0) -0.148
Half life (OD (600 nm) = 0.3, 
M9 media, 36C; min)
1200 View in model
 
Synthesis
Localization c View in model
 
Comments
Comments first observed N-terminal residue by mass-spec 19 [PUB_0280] Functional Macromolecule Functional as monomer [PUB_0037]. Coenzymes Interacts with 2 MN per monomer as prosthetic group [96].
References
  1. Gupta N, Tanner S, Jaitly N, Adkins JN, Lipton M, Edwards R, Romine M, Osterman A, Bafna V, Smith RD, Pevzner PA. Whole proteome analysis of post-translational modifications: applications of mass-spectrometry for proteogenomic annotation. Genome Res 17, 1362-77 (2007). WholeCell: PUB_0280, PubMed: 17690205

  2. 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 15:07:58
Last updated 2012-10-01 15:14:42