3.4.15.1: peptidyl-dipeptidase A

This is an abbreviated version!
For detailed information about peptidyl-dipeptidase A, go to the full flat file.

Reaction

release of a C-terminal dipeptide, oligopeptide-/-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II =

Synonyms

ACE, ACE-1, ACE2, ACEI, ANCE, ANG I-converting enzyme, angiotensin 1 converting enzyme, angiotensin converting enzyme, angiotensin converting enzyme 1, angiotensin converting enzyme I, angiotensin converting enzyme inhibitor, angiotensin I converting enzyme, angiotensin I-converting enzyme, angiotensin-converting enzyme, angiotensin-converting enzyme 2, angiotensin-converting enzyme type 1, angiotensin-converting enzyme-2, angiotensin-converting-enzyme, angiotensin-I converting enzyme, angiotensin-I-converting enzyme, carboxycathepsin, carboxypeptidase, dipeptidyl, CD143, CD143 antigen, crab-ACE, DCP, Dcp1, Dipeptidyl carboxypeptidase, dipeptidyl carboxypeptidase I, dipeptidylcarboxypeptidase, endothelial cell peptidyl dipeptidase, gACE, germinal ACE, kinases II peptidyldipeptide hydrolase, kininase II, mACE2, More, PDH, peptidase P, peptidyl dipeptidase, peptidyl dipeptidase A, peptidyl dipeptidase I, peptidyl dipeptidase-4, peptidyl dipeptide hydrolase, peptidyl-dipeptide hydrolase, peptidyldipeptide hydrolase, rhACE2, s-ACE, sACE, sACE-1, somatic ACE, somatic angiotensin I-converting enzyme, TACE, testicular ACE, testis ACE, XcACE, zinc dipeptidyl carboxypeptidase, Zn2+ peptidyldipeptidase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.15 Peptidyl-dipeptidases

                3.4.15.1 peptidyl-dipeptidase A

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Results	in table
30	Activating Compound
189	AA Sequence
65	Application
1	CAS Registry Number
25	Cloned(Commentary)
12	Crystallization (Commentary)
65670	Disease/ Diagnostics
2	Expression
54	General Information
3	General Stability
411	IC50 Value
1153	Inhibitors
1	kcat/KM [mM/s]
307	Ki Value [mM]
249	KM Value [mM]
51	Localization
68	Metals/Ions
81	Molecular Weight [Da]
98	Natural Substrates/ Products (Substrates)
739	Organism
132	PDB ID
54	pH Optimum
8	pH Range
3	pH Stability
3	pI Value
49	Posttranslational Modification
39	Protein Variants
51	Purification (Commentary)
1	Reaction
1	Reaction Type
407	Reference
429	Source Tissue
45	Specific Activity [micromol/min/mg]
6	Storage Stability
535	Substrates and Products (Substrate)
56	Subunits
338	Synonyms
37	Temperature Optimum [°C]
1	Temperature Range [°C]
17	Temperature Stability [°C]
172	Turnover Number [1/s]

Subunits

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Subunits on EC 3.4.15.1 - peptidyl-dipeptidase A

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

?

36 entries

dimer

Homo sapiens

P12821

the N domain of ACE influences domain shedding and enzyme dimerization, overview. Epitope mapping using monoclonal antibodies directed to the N domain of ACE, overview

710612

monomer

6 entries

trimer

Sus scrofa

-

3 * 70000, SDS-PAGE after treatment with 2-mercaptoethanol

81262

additional information

10 entries

?

Bacillus pumilus

-

x * 70000, SDS-PAGE

81285

?

Bacillus pumilus HL721

-

x * 70000, SDS-PAGE

-

?

Bos taurus

-

x * 126000, denatured and reduced denatured enzyme, SDS-PAGE

81271

?

Bos taurus

-

x * 126000, enzyme from lung, SDS-PAGE with 7% acryl amide

81211

?

Bos taurus

-

x * 180000, electrophoresis under denaturing conditions

650267

?

Canis lupus familiaris

-

x * 140000, enzyme from lung, SDS-PAGE with 7% acryl amide

81211

?

Homo sapiens

-

-

81209

?

Homo sapiens

-

x * 140000, SDS-PAGE

81248

?

Homo sapiens

-

x * 140000, enzyme from plasma, SDS-PAGE with 7% acryl amide

81211

?

Homo sapiens

-

x * 150000, SDS-PAGE in presence of 2-mercaptoethanol

81235

?

Homo sapiens

-

x * 170000, kidney, SDS-PAGE of the reduced enzyme

81242

?

Homo sapiens

-

x * 170000, lung enzyme, SDS-PAGE

81231

?

Homo sapiens

-

x * 170000, kidney enzyme, SDS-PAGE

81212

?

Homo sapiens

-

x * 160000, lung and kidney enzyme, SDS-PAGE with or without 1% 2-mercaptoethanol

81236

?

Homo sapiens

-

major protein bands of 55000 Da and 65000 Da, and minor protein bands of about 90000 Da and 140000 Da, SDS-PAGE under reducing conditions

81280

?

Homo sapiens

-

x * 165000, SDS-PAGE with 5% acryl amide

81211

?

Homo sapiens

-

x * 150000, PAGE under denaturing conditions

81234

?

Homo sapiens

-

x * 55000 + x * 65000, SDS-PAGE

81232

?

Homo sapiens

-

x * 130000, enzyme from lung, SDS-PAGE with 7% acryl amide

81211

?

Oryctolagus cuniculus

-

-

81257

?

Oryctolagus cuniculus

-

x * 140000, enzyme from plasma, SDS-PAGE with 7% acryl amide

81211

?

Oryctolagus cuniculus

-

x * 180000, enzyme from lung, SDS-PAGE with 5% acryl amide

81211

?

Oryctolagus cuniculus

-

x * 140000, enzyme from lung, SDS-PAGE with 7% acryl amide

81209, 81211

?

Oryctolagus cuniculus

-

x * 140000, enzyme from lung, in reduced and denatured state, SDS-PAGE

81227, 81259

?

Oryctolagus cuniculus

-

x * 128500, equilibrium sedimentation under denaturing conditions

81259

?

Oryctolagus cuniculus

-

x * 100000, enzyme from testis, in reduced and denatured state, SDS-PAGE

81227

?

Rattus norvegicus

-

x * 91000, SDS-PAGE

81255

?

Rattus norvegicus

-

x * 139000, SDS-PAGE with 7% acryl amide

81211

?

Rattus norvegicus

-

x * 165000, SDS-PAGE

81252

?

Sus scrofa

-

-

81209

?

Sus scrofa

-

x * 139000, SDS-PAGE with 7% acryl amide

81211

?

Sus scrofa

-

x * 180000, one enzyme form from striatum and kindey enzyme

81266

?

Sus scrofa

-

x * 195000, enzyme from kidney, SDS-PAGE with 5% acryl amide

81211, 81261

?

Sus scrofa

-

x * 206000, enzyme from lung, SDS-PAGE with 5% acryl amide

81211

?

Sus scrofa

-

x * 206000, SDS-PAGE

81262

?

Sus scrofa

-

x * 170000, one enzyme form from striatum, SDS-PAGE

81265, 81266

monomer

Alitta virens

-

1 * 71000, SDS-PAGE

650873

monomer

Homo sapiens

-

1 * 145000, enzyme in reduced and unreduced samples, SDS-PAGE

81245

monomer

Homo sapiens

-

1 * 155000, enzyme from kidney and lung, SDS-PAGE in presence of 2-mercaptoethanol

81213

monomer

Homo sapiens

P12821

1 * 138000, calculated from sequence, 1 * 170000, SDS-PAGE

764572

monomer

Pseudomonas sp.

-

1 * 74000, SDS-PAGE

81286

monomer

Pseudomonas sp. WO24

-

1 * 74000, SDS-PAGE

-

additional information

Homo sapiens

-

-

81280

additional information

Homo sapiens

P12821

ACE comprises two homologous domains, that differ in their substrate preferences, overview. Has a similar binding mode like its parent compound lisinopril, but the P2' tryptophan moiety takes a different conformation to that seen in other inhibitors having a tryptophan residue in this position

707443

additional information

Homo sapiens

-

ACE comprises two homologous domains, that differ in their substrate preferences, overview. Has a similar binding mode like its parent compound lisinopril, but the P2' tryptophan moiety takes a different conformation to that seen in other inhibitors having a tryptophan residue in this position

707443

additional information

Homo sapiens

-

isozyme domain structures with N- and C-domains and the HEXXH motif, overview

708830

additional information

Homo sapiens

-

the N- and C-domains of ACE shows a deep active site cleft and a lid region that restrict access of substrates or inhibitors until a conformational change of the enzyme occurs, binding of ACE inhibitors to one domain can alter the other

708687

additional information

Homo sapiens

P12821

the protein seems mostly monomeric in solution, but the dimer is detected in both 2D and 3D cryo-EM reconstruction

764572

additional information

Leishmania donovani

Q4KXL2

enzyme homology modelling, overview

709284

additional information

Leishmania donovani

-

enzyme homology modelling, overview

709284

additional information

Oryctolagus cuniculus

-

ACE structure-activity relationship, overview

707653

additional information

Rattus norvegicus

-

ACE contains transactivation domains in its sequence

709149