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
-
3.4.23.32
-
subsite
-
dyad
-
scissile
-
beta-sandwich
-
rhythm
-
canaliculatum
-
ventricles
-
commenced
-
busycon
-
chymotrypsin
-
oxyanion
-
metoclopramide
-
atrial
-
aspergillopepsin
-
excitatory
-
neuromodulation
-
tetrahedral
-
whelk
-
beat
-
methysergide
- 3.4.23.32
-
subsite
-
dyad
-
scissile
-
beta-sandwich
-
rhythm
- canaliculatum
-
ventricles
-
commenced
- busycon
- chymotrypsin
-
oxyanion
- metoclopramide
-
atrial
- aspergillopepsin
-
excitatory
-
neuromodulation
-
tetrahedral
- whelk
-
beat
- methysergide
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
Advanced search results
Crystallization
Crystallization on EC 3.4.23.32 - Scytalidopepsin B
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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
-
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
-
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
-