3.4.22.47: gingipain K

This is an abbreviated version!
For detailed information about gingipain K, go to the full flat file.

Reaction

endopeptidase with strict specificity for lysyl bonds =

Synonyms

gingipain, gingipain K, HbR, K-gingipain, K-specific gingipain protease, KGP, Lys-gingipain, Lys-specific cysteine proteinase gingipain, lysine gingipain, lysine-sepcific cysteine protease, lysine-specific gingipain, lysine-specific gingipain K, lysine-specific gingipain protease, lysine-specific gingipain proteinase, lysine-specific proteinase, porphypain, PrtP proteinase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.22 Cysteine endopeptidases

                3.4.22.47 gingipain K

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Results	in table
15	Activating Compound
59	AA Sequence
7	Application
1	CAS Registry Number
5	Cloned(Commentary)
3	Crystallization (Commentary)
14	General Information
1	General Stability
53	Inhibitors
3	Ki Value [mM]
7	KM Value [mM]
14	Localization
1	Metals/Ions
10	Molecular Weight [Da]
33	Natural Substrates/ Products (Substrates)
126	Organism
7	PDB ID
21	pH Optimum
1	pH Range
3	pH Stability
4	Posttranslational Modification
18	Protein Variants
11	Purification (Commentary)
3	Reaction
1	Reaction Type
65	Reference
6	Source Tissue
3	Specific Activity [micromol/min/mg]
105	Substrates and Products (Substrate)
15	Subunits
93	Synonyms
19	Temperature Optimum [°C]
6	Temperature Stability [°C]
1	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.22.47 - gingipain K

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

sitting drop vapor diffusion method

Porphyromonas gingivalis

Q51817

754156

sitting-drop vapor diffusion method, high-resolution (1.20 A) complex structure of the enzyme with KYT-36. Sub-nanomolar inhibition of Kgp is achieved by tight binding to the active-site cleft, which is covered for its sub-sites S3 through S1' under establishment of nine hydrophobic interactions, 14 hydrogen bonds and one salt bridge. In addition, an inhibitor carbonyl carbon that mimics the scissile carbonyl of substrates is pyramidalized and just 2.02 A away from the catalytic nucleophile of Kgp, C477Sgamma

Porphyromonas gingivalis

Q51817

755522

the crystal structure of a domain within the haemagglutinin region of Kgp is reported here. The K2 domain structure is a jellyroll fold with two anti-parallel beta-sheets. This fold topology is shared with adhesive domains from functionally diverse receptors such as MAM domains, ephrin receptor ligand binding domains and a number of carbohydrate binding modules

Porphyromonas gingivalis

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710002