KEGG ENZYME: 3.4.11.24

ENZYME: 3.4.11.24

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

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

PMEX:

H4W19_05095

LAB:	LA76x_2290

LAQ:	GLA29479_4741

LYJ:	FKV23_08410

LSOL:

GOY17_10765

LSX:	H8B22_14355

LARE:

HIV01_005740

LAUX:

LA521A_20980

AEI:	AOY20_13825

ALA:	BFG52_11235

ACUM:

C9E88_015075

ADS:	FPL17_04915

ALJ:	G8D99_10180

AWG:	GFH30_08895

ASHA:

G8E00_06040

AGYL:

FPL18_16740

APOT:

MZO21_08355

APRL:

PY247_16435

AVIV:

LF296_09075

SCO:	SCO4589(SCD20.07c)

SALB:

XNR_0958

SMA:	SAVERM_4872(lap)

SGR:

SGR_5809

SGB:

WQO_06245

SFI:

SFUL_1215

SANL:

KZO11_05925

SGRF:

SGFS_071140

SCYE:

R2B67_30195

SCB:	SCAB_37611

SSX:	SACTE_1130

SVL:	Strvi_0799 Strvi_3541

SHY:

SHJG_6556

SHO:	SHJGH_6316

SRC:	M271_07785 M271_22010

SMAL:

SMALA_4385 SMALA_6876

SSOI:

I1A49_26000 I1A49_38160

SFA:

Sfla_5137

SBH:

SBI_06122

SVE:

SVEN_4288

SALS:

SLNWT_4508

STRP:

F750_1501

SLV:	SLIV_15325(lieA)

SGU:	SGLAU_02315(lieA)

SVT:	SVTN_22375

STRE:

GZL_01334

SLD:

T261_0522

SLC:	SL103_20730

SXI:	SXIM_11980

STRM:

M444_20415

STRC:

AA958_10130

SAMB:

SAM23877_4424

SPRI:

SPRI_3253

SCZ:	ABE83_29585

SCX:	AS200_20810

STRF:

ASR50_23025

SRN:	A4G23_03276(lieA)

SPAV:

Spa2297_19400

SCLF:

BB341_10770

STSI:

A4E84_23880

SKY:	D0C37_06180

SALW:

CP975_28260

SGM:	GCM10017557_48620

SCAD:

DN051_05370

SPHW:

NFX46_03370 NFX46_33130

SLS:	SLINC_4975

SNR:	SNOUR_05855(lieA)

SALU:

DC74_7273

SALL:

SAZ_37685

STRD:

NI25_13800 NI25_16020

SNW:	BBN63_13330

SAUO:

BV401_25760 BV401_38020

SSIA:

A7J05_08725

SVU:	B1H20_05425

SGV:	B1H19_36750

SLAU:

SLA_4407

SALF:

SMD44_05158

SALJ:

SMD11_3785

SLX:	SLAV_16255(lieA2)

STRO:

STRMOE7_34925

SFK:	KY5_4733c KY5_6276c

SNZ:	DC008_20335

SGE:	DWG14_00558 DWG14_03523(lieA_2)

SLK:	SLUN_23515

SGD:	ELQ87_16250

SQZ:	FQU76_20285

SCYA:

EJ357_27295

SAST:

CD934_11525

STIR:

DDW44_17555

SKA:	CP970_09635 CP970_17755

SGZ:	C0216_02600

SVN:	CP980_14235

SHAW:

CEB94_24245

SRK:	FGW37_14515

SFIC:

EIZ62_13370

SGAL:

CP966_11220 CP966_21505

SSPO:

DDQ41_18595

SPAD:

DVK44_12355

SFY:	GFH48_17805

SAQU:

EJC51_28720

SCAV:

CVT27_05075

SBY:	H7H31_01220 H7H31_13515

SRIM:

CP984_21950 CP984_37305

SSUB:

CP968_14400

SPHV:

F9278_30210

SCIN:

CP977_20280

SFUG:

CNQ36_22895

SPAC:

B1H29_15430

STSU:

B7R87_19850

SCHA:

CP983_17910

SGX:	H4W23_23720

SCOE:

CP976_25690

SBAT:

G4Z16_31110

SSPB:

CP982_24865

SNF:	JYK04_05033(lieA_1) JYK04_07384

SPLA:

CP981_35425

STUI:

GCM10017668_41790

SATA:

C5746_31225

SHUN:

DWB77_03282(lieA)

SHAR:

HUT13_06765

SFEU:

IM697_41075

SLIA:

HA039_13765

SDW:	K7C20_34175

SCAL:

I6J39_05595

SAUH:

SU9_031695

SFB:	CP974_17765

SMOB:

J7W19_14225

SPEU:

CGZ69_20715

SROI:

IAG44_16440

SGJ:	IAG43_18440

SHK:	J2N69_29465

SANU:

K7396_02195

SDD:	D9753_27265

SACT:

DMT42_01750

SGOB:

test1122_26150

SINE:

KI385_39865

SLF:	JEQ17_27395

SDEC:

L3078_27775

SAOV:

G3H79_14895

SDUR:

M4V62_11140 M4V62_18650

SYAN:

NRK68_19840

SAKB:

K1J60_17650

STAA:

LDH80_17120

SNIG:

HEK616_39790

SVIO:

HWN34_05455

SCAE:

IHE65_17845

STUB:

MMF93_03550

SSPN:

LXH13_17725

SCIR:

STRCI_000108 STRCI_004779

SXT:	KPP03845_104430(lieA_1)

STUD:

STRTU_000377

SENG:

OJ254_24940

SGK:	PET44_19110

SANT:

QR300_06850 QR300_19300

SYUN:

MOV08_05780

SJN:	RI060_16665

SOV:	QZH56_19835

SFIY:

F0344_29960

SHAU:

K9S39_02925

SKG:	KJK29_14585

SCOA:

QU709_16930

SROC:

RGF97_13095

SFP:	QUY26_15790

SCHG:

NRO40_17640

STTN:

BSL84_19620

STRZ:

OYE22_01310 OYE22_13320

KAB:	B7C62_05135

AGLA:

OIE69_06965

ARU:	ASPU41_14755 ASPU41_18675

ARQ:	BWQ92_21955

ACRY:

AC20117_14545 AC20117_15825

ASUF:

MNQ99_11185 MNQ99_16300

LMOI:

VV02_18030

BEI:	GCM100_11610

TDF:	H9L22_00700

MUZ:	H4N58_12095

SGRG:

L0C25_10600 L0C25_18785

KFL:

Kfla_5609

KQI:	F1D05_12270

AGRA:

AGRA3207_002060 AGRA3207_003417

AMAZ:

LUW76_21940

ACIR:

OG979_14815

SPIQ:

OHA34_25840

SRO:

Sros_0792

NOA:	BKM31_41640

NCX:	Nocox_23525

NGN:	LCN96_03670

NFS:	OIE67_43130

SEN:

SACE_5205

AMD:

AMED_1036

AMN:

RAM_05270

AMM:

AMES_1032

AMZ:

B737_1033

AOI:

AORI_1025

AJA:	AJAP_34460

AMYC:

CU254_16950

AMYB:

BKN51_39230

AAB:	A4R43_20210

AMYY:

YIM_09430(lieA2)

AORI:

SD37_36070

APRT:

MUY14_31605

AROO:

NQK81_17755

ARHD:

VSH64_42760

PSEA:

WY02_27520

PSEE:

FRP1_21215

PSEQ:

AD006_00400

PECQ:

AD017_08225

PHH:	AFB00_00440

APRE:

CNX65_24430

AMI:

Amir_4953

SESP:

BN6_58410(lieA)

SSYI:

EKG83_20115 EKG83_38670

KBU:	Q4V64_30850

KPHY:

AOZ06_01175 AOZ06_30780 AOZ06_38895

LED:	BBK82_23070

ALO:	CRK55046 CRK58695

SACE:

GIY23_14480

ACTU:

Actkin_01195(lieA_3) Actkin_05450(lieA_8)

CROS:

N8J89_14005 N8J89_29685 N8J89_29690

UME:	RM788_15810 RM788_46995

STP:	Strop_1408

SAQ:

Sare_1367

MAU:	Micau_2351

MIL:

ML5_2463

MICB:

MicB006_5416

MTUA:

CSH63_13000

MICH:

FJK98_16960

MTEM:

GCE86_05215

MCAB:

HXZ27_14170

MSAG:

GCM10017556_56230

VMA:	VAB18032_19160

VER:	HUT12_08535

MENO:

Jiend_56490

ASE:

ACPL_3300

AMS:	AMIS_36460

ACTN:

L083_5601

AFS:

AFR_35720

ACTS:

ACWT_3172

AIH:	Aiant_68920

ACTR:

Asp14428_63040 Asp14428_74090

ASIC:

Q0Z83_061700

AOU:	ACTOB_002331 ACTOB_004045

PLAB:

C6361_02130

PLAT:

C6W10_19540

PFLA:

Pflav_059630

PSUU:

Psuf_020360

CATI:

CS0771_34570 CS0771_35120

DFU:	Dfulv_37460

CCAZ:

COUCH_08675

SNA:

Snas_5560

BVO:	Pan97_33690(ywaD_1)

LPAV:

PLANPX_2384

GPN:	Pan110_51830

SDYN:

Mal52_50570

PLON:

Pla110_35370(lieA)

ACAF:

CA12_18400(lieA)

PFER:

IRI77_10690

HCU:	MUN79_15630

NOJ:	EJ995_05055

ELB:	VO54_01494(lieA)

MEMA:

MMAB1_3205

» show all

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)
DOI:10.1107/S0907444900002420

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

All links

Gene (300)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (294)   
   RefGene (5)   
Protein sequence (525)   
   UniProt (521)   
   SWISS-PROT (1)   
   RefSeq(pep) (3)   
DNA sequence (568)   
   RefSeq(nuc) (5)   
   GenBank (281)   
   EMBL (282)   
Protein domain (5)   
   InterPro (5)   
All databases (1398)   

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