3.4.11.15: aminopeptidase Y

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For detailed information about aminopeptidase Y, go to the full flat file.

Reaction

preferentially, release of N-terminal lysine =

Synonyms

AAP, aminopeptidase (cobalt-activated), aminopeptidase Co, APE3, LapB, lysine aminopeptidase, PF1861, PH1821, PhTET3, TET3, yylAPE

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.11 Aminopeptidases

                3.4.11.15 aminopeptidase Y

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Results	in table
3	Activating Compound
256	AA Sequence
1	CAS Registry Number
3	Cloned(Commentary)
2	Crystallization (Commentary)
2	Expression
1	General Information
2	General Stability
1	IC50 Value
48	Inhibitors
5	kcat/KM [mM/s]
7	KM Value [mM]
8	Localization
17	Metals/Ions
14	Molecular Weight [Da]
3	Natural Substrates/ Products (Substrates)
18	Organism
3	PDB ID
9	pH Optimum
2	pH Range
1	pH Stability
1	pI Value
5	Posttranslational Modification
1	Protein Variants
6	Purification (Commentary)
1	Reaction
1	Reaction Type
18	Reference
6	Specific Activity [micromol/min/mg]
65	Substrates and Products (Substrate)
10	Subunits
15	Synonyms
6	Temperature Optimum [°C]
1	Temperature Range [°C]
5	Temperature Stability [°C]
5	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.11.15 - aminopeptidase Y

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

the 12-subunit PhTET3 complex is crystallized and its 3D structure is solved at a resolution of 1.9 A by molecular replacement

Pyrococcus horikoshii

O59485

723211

x-ray crystal structure of the Co(II)-loaded form ([CoCo(AAP)]) is solved to 2.2 A resolution. [CoCo(AAP)] folds into an alpha/beta globular domain with a twisted beta-sheet hydrophobic core sandwiched between alpha-helices, identical to [ZnZn(AAP)]. Tris(hydroxymethyl)aminomethane coordinates to the dinuclear Co(II) active site of AAP with one of the Tris hydroxyl oxygen atoms (O4) forming a single oxygen atom bridge between the two Co(II) ions. This is the only Tris atom coordinated to the metals with Co1-O and Co2-O bonds distances of 2.2 and 1.9 A, respectively. Each of the Co(II) ions resides in a distorted trigonal bipyramidal geometry

Vibrio proteolyticus

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683745