KEGG   ENZYME: 3.4.11.24Help
Entry
EC 3.4.11.24                Enzyme                                 

Name
aminopeptidase S;
Mername-AA022 peptidase;
SGAP;
aminopeptidase (Streptomyces griseus);
Streptomyces griseus aminopeptidase;
S. griseus AP;
double-zinc aminopeptidase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Aminopeptidases
BRITE hierarchy
Reaction(IUBMB)
Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues
Comment
Aminopeptidases are associated with many biological functions, including protein maturation, protein degradation, cell-cycle control and hormone-level regulation [3,4]. This enzyme contains two zinc molecules in its active site and is activated by Ca2+ [4]. In the presence of Ca2+, the best substrates are Leu-Phe, Leu-Ser, Leu-pNA (aminoacyl-p-nitroanilide), Phe-Phe-Phe and Phe-Phe [3]. Peptides with proline in the P1' position are not substrates [3]. Belongs in peptidase family M28.
History
EC 3.4.11.24 created 2008
Orthology
K19702  aminopeptidase S
Genes
LAB: LA76x_2290
LAQ: GLA29479_4741
AEI: AOY20_13825
ALA: BFG52_11235
SCO: SCO4589(SCD20.07c)
SMA: SAVERM_4872(lap)
SGR: SGR_5809
SGB: WQO_06245
SCB: SCAB_37611
SSX: SACTE_1130
SFA: Sfla_5137
SBH: SBI_06122
SHY: SHJG_6556
SVE: SVEN_4288
SALB: XNR_0958
SALS: SLNWT_4508
STRP: F750_1501
SFI: SFUL_1215
SALU: DC74_7273
SALL: SAZ_37685
SLV: SLIV_15325(lieA)
SGU: SGLAU_02315(lieA)
STRE: GZL_01334
SLD: T261_0522
STRM: M444_20415
SPRI: SPRI_3253
SRN: A4G23_03276(lieA)
SNR: SNOUR_05855(lieA)
SALJ: SMD11_3785
SLX: SLAV_16255(lieA2)
LMOI: VV02_18030
KFL: Kfla_5609
SRO: Sros_0792
SEN: SACE_5205
AMD: AMED_1036
AMN: RAM_05270
AMM: AMES_1032
AMZ: B737_1033
AOI: AORI_1025
PSEA: WY02_27520
PSEE: FRP1_21215
AMI: Amir_4953
SESP: BN6_58410(lieA)
SAQ: Sare_1367
MIL: ML5_2463
AFS: AFR_35720
ACTS: ACWT_3172
SNA: Snas_5560
ELB: VO54_01494(lieA)
 » show all
Taxonomy
Reference
1  [PMID:2503378]
  Authors
Spungin A, Blumberg S.
  Title
Streptomyces griseus aminopeptidase is a calcium-activated zinc metalloprotein. Purification and properties of the enzyme.
  Journal
Eur J Biochem 183:471-7 (1989)
DOI:10.1111/j.1432-1033.1989.tb14952.x
  Sequence
[sgr:SGR_5809]
Reference
2  [PMID:8444149]
  Authors
Ben-Meir D, Spungin A, Ashkenazi R, Blumberg S.
  Title
Specificity of Streptomyces griseus aminopeptidase and modulation of activity by divalent metal ion binding and substitution.
  Journal
Eur J Biochem 212:107-12 (1993)
DOI:10.1111/j.1432-1033.1993.tb17639.x
  Sequence
[sgr:SGR_5809]
Reference
3  [PMID:16080009]
  Authors
Arima J, Uesugi Y, Iwabuchi M, Hatanaka T.
  Title
Study on peptide hydrolysis by aminopeptidases from Streptomyces griseus, Streptomyces septatus and Aeromonas proteolytica.
  Journal
Appl Microbiol Biotechnol 70:541-7 (2006)
DOI:10.1007/s00253-005-0105-8
Reference
4  [PMID:15280041]
  Authors
Fundoiano-Hershcovitz Y, Rabinovitch L, Langut Y, Reiland V, Shoham G, Shoham Y.
  Title
Identification of the catalytic residues in the double-zinc aminopeptidase from Streptomyces griseus.
  Journal
FEBS Lett 571:192-6 (2004)
DOI:10.1016/j.febslet.2004.07.001
Reference
5  [PMID:10771423]
  Authors
Gilboa R, Greenblatt HM, Perach M, Spungin-Bialik A, Lessel U, Wohlfahrt G, Schomburg D, Blumberg S, Shoham G.
  Title
Interactions of Streptomyces griseus aminopeptidase with a methionine product analogue: a structural study at 1.53 A resolution.
  Journal
Acta Crystallogr D Biol Crystallogr 56:551-8 (2000)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.11.24
IUBMB Enzyme Nomenclature: 3.4.11.24
ExPASy - ENZYME nomenclature database: 3.4.11.24
BRENDA, the Enzyme Database: 3.4.11.24

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