Proteinase

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Proteinase (PRO) are enzymes which hydrolyze peptide bonds. They are classified by the amino acid site of their cleavage or by the pH at which they are active. PRO B is a serine protease. For more details on PRO B see Streptomyces griseus proteinase B. PRO A is a carboxylproteinase. PRO K is a serine protease which cleaves proteins preferentially after hydrophobic residues. Calcium ions contribute to the stability of the enzyme. PRO K is active over a wide pH range and is used in molecular biology to inactivate nucleases from preparations of DNA or RNA. PRO K is used in the partial proteolysis of lactoferrin into its N- and C-lobe. The two lobes of lactoferrin have different antimicrobial and antifungal properties. PRO K can digest hair (keratin).

3D structures of proteinase

Updated on 30-May-2025

PRO A

2sga – SgPRO – Streptomyces griseus

2jxr, 1fmu, 1fmx – yPRO - yeast
1sgc - SgPRO + chymostatin A
3sga, 4sga, 5sga - SgPRO + polypeptide inhibitor
1dp5, 1dpj, 1g0v - yPRO + polypeptide inhibitor IA3
1fq5 - yPRO + inhibitor

PRO B

3sgb – SgPRO + turkey ovomucoid inhibitor

1sgp, 1sgq, 1sgr, 1cso, 1ct0, 1ct2, 1ct4, 1ds2, 2sgp, 2nu3, 2nu4 – SgPRO + turkey ovomucoid inhibitor (mutant)
4sgb - SgPRO + potato inhibitor

PRO K

2prk, 1cnm, 1egq, 2id8, 2g4v, 2v8b, 3gt3, 3gt4, 3d9q, 3ddz, 3de0 , 3de1, 3de2, 3de3, 3de4, 3de5, 3de6, 3de7, 3dvq, 3dvr, 3dvs, 3dw1, 3dw3, 3dwe, 3i2y, 3i30, 3i37, 3i34, 3l1k, 3aj8, 3aj9, 3q40, 3q5g, 3qmp, 4b5l, 4fon – EaPRO + Ca – Engyodontium album

1ic6 – EaPRO (mutant) + Ca
1ptk, 1ht3 – EaPRO + Ca + Hg
2pkc – EaPRO + Na
4dj5 – EaPRO

PRO K complex with peptide

3prk, 1p7v, 1p7w – EaPRO + Ca + peptide inhibitor

1bjr, 2dqk, 2duj – EaPRO + Ca + lactoferrin peptide
2hd4 – EaPRO + Ca + lactoferrin peptide inhibitor
2dp4, 3ptl – EaPRO + lactoferrin peptide
1pek, 1pfg – EaPRO + peptide inhibitor
1pj8 – EaPRO + Hg + substrate analog peptide
2hpz, 2pq2 – EaPRO + Ca + peptide
3osz – EaPRO + Ca + antimicrobial peptide
2b6n – PRO + tripeptide - Serratia

PRO K complex with small molecule

2pwb – EaPRO + Ca + coumarin

2pyz – EaPRO + Ca + auramine
2pwa – EaPRO + Ca + alanine boronic acid
1oyo – EaPRO + Ca + melanin monomer
3dyb – EaPRO + Ca + digalacturonic acid

PRO 3C

1qa7 – PRO – Hepatitis virus

2vb0 - PRO – Coxsakievirus

H2-PRO

1wni – PRO – Trimeresurus flavoviridis

Aspartic PRO

2asi – PRO – Rhizomucor miehei

1zap – CaPRO – Candida albicans
1izd - AoPRO – Aspergillus oryzae
1eag – CaPRO + inhibitor
1fq4 - yPRO + inhibitor
1j71 - PRO + polypeptide inhibitor – Candida tropicalis
1ize - AoPRO + polypeptide-statine inhibitor
1wkr - PRO + polypeptide-statine inhibitor – Irpex lacteus

Cysteine PRO

2hrv – PRO 2A – human rhinovirus

Serine PRO

1s2n, 1sh7 – PRO – Vibrio

3s9a, 3s9b – RvPRO – Siamese Russell’s viper
3s9c, 3sbk – RvPRO + human factor V polypeptide
1ga1, 1ga4, 1ga6, 1nlu – PsPRO + iodotyrostatin fragment – Pseudomonas
1kdv, 1kdy, 1kdz, 1ke1, 1ke2 - PsPRO + polypeptide inhibitor




E. coli proteinase K complex with lactoferrin peptide and Ca+2 (PDB code 2duj)

Drag the structure with the mouse to rotate

ReferencesReferences

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Michal Harel, Alexander Berchansky, Joel L. Sussman, Karsten Theis