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3.4.23.32: Scytalidopepsin B

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

Word Map on EC 3.4.23.32

Reaction

Hydrolysis of proteins with broad specificity, cleaving Phe24-/-Phe, but not Leu15-Tyr and Phe25-Tyr in the B chain of insulin =

Synonyms

eqolisin, Ganoderma lucidum carboxyl proteinase, More, Proteinase, Ganoderma lucidum aspartic, Proteinase, Scytalidium lignicolum aspartic, B, SCP-B, Scytalidium aspartic proteinase B, Scytalidium lignicolum pepstatin-insensitive carboxyl peptidase, Scytalido-carboxyl peptidase-B, scytalidoglutamic peptidase, SGP, SLB

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.32 Scytalidopepsin B

Crystallization

Crystallization on EC 3.4.23.32 - Scytalidopepsin B

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme-(acetyl-FKF-(3S,4S)-phenylstatinyl)-LR-NH2 complex and enzyme-acetyl-FKF(2R,3S)-phenylisoseryl-ALR-NH2 complex. Native crystals of the enzyme are grown at room temperature by the hanging-drop vapor diffusion method from 42% saturated ammonium sulfate, 10% ethylene glycol and 0.1 M sodium acetate buffer (pH 4.0). These crystals are then soaked in solutions of varying concentrations of the transition state analogs (acetyl-FKF-(3S,4S)-phenylstatinyl)-LR-NH2 and acetyl-FKF(2R,3S)-phenylisoseryl-ALR-NH2
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purified enzyme complexed with angiotensin II, hanging drop method, room temperature, from 42% saturated ammonium sulfate, 0.1 M sodium acetate, pH 4.0, 10% v/v ethylene glycol, crystals are soaked in cryosolution containing 30% glvcerol, 45% saturated ammonium sulfate,and 0.1 M sodium acetate, pH 4.0, heavy atom derivatizing, X-ray diffraction structure determination and analysis at 1.9-2.5 A resolution, molecular modeling and multiple isomorphous replacement phasing
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the three-dimensional structure of SGP is determined by X-ray crystallography. The polypeptide folds into a beta-sandwich that has seven antiparallel beta-strands in each of the two sheets
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