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Literature summary for 1.14.11.4 extracted from

  • Chen, Y.; Terajima, M.; Banerjee, P.; Guo, H.; Liu, X.; Yu, J.; Yamauchi, M.; Kurie, J.M.
    FKBP65-dependent peptidyl-prolyl isomerase activity potentiates the lysyl hydroxylase 2-driven collagen cross-link switch (2017), Sci. Rep., 7, 46021 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.11.4

Activating Compound

Activating Compound Comment Organism Structure
FKBP65 FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2. Reconstitution with wild-type FKBP65 increases the enzyme activity by 7fold Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum
-
 Mus musculus 5783
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2 ?
-
 ?
[procollagen]-L-lysine + 2-oxoglutarate + O2 Mus musculus
-
 [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus Q9R0B9
-
-

Source Tissue

Source Tissue Comment Organism Textmining
embryo
-
 Mus musculus
-
fibroblast
-
 Mus musculus
-
MEF cell
-
 Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2 Mus musculus ?
-
 ?
[procollagen]-L-lysine + 2-oxoglutarate + O2
-
 Mus musculus [procollagen]-(2S,5R)-5-hydroxy-L-lysine + succinate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
LH2
-
 Mus musculus
lysyl hydroxylase 2
-
 Mus musculus
PLOD2
-
 Mus musculus

General Information

General Information Comment Organism
physiological function LH2 promotes fibrosis and cancer metastasis. Peptidyl prolyl isomerase (PPIase) activity of FKBP65 positively modulates LH2 enzymatic activity and is critical for the formation of hydroxylysine-aldehyde derived intermolecular collagen cross-links. FKBP65 regulates LH2-mediated collagen cross-linking. FKBP65 interacts with LH2 through its peptidyl prolyl isomerase (PPIase) domains, FKBP65 forms a complex with LH2. Reconstitution with wild-type FKBP65 increases the enzyme activity by 7fold Mus musculus