3.4.23.15: renin

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

Word Map on EC 3.4.23.15

3.4.23.15

hypertension

aldosterone

arterial

urinary

cardiovascular

cardiac

antihypertensive

normotensive

gastric

glomerular

natriuretic

hemodynamic

systolic

diastolic

sympathetic

ras

angiotensin-converting

norepinephrine

output

adrenal

blocker

prostaglandin

ventricular

catecholamine

diuretic

creatinine

hg

electrolyte

placebo

vasopressin

captopril

vasodilator

cortisol

supine

intrarenal

renovascular

conscious

pressor

posture

acth

noradrenaline

losartan

hypotensive

mineralocorticoid

vasoconstriction

enalapril

furosemide

anp

medicine

macula

pharmacology

aceis

diagnostics

Reaction

cleavage of Leu-/- bond in angiotensinogen to generate angiotensin I =

Synonyms

angiotensin-forming enzyme, angiotensinogenase, EC 3.4.4.15, EC 3.4.99.19, prorenin, REN, SVAP, SVAP A1, SVAP B1, SVAP B2, venom aspartic protease

ECTree

3 Hydrolases

3.4 Acting on peptide bonds (peptidases)

3.4.23 Aspartic endopeptidases

3.4.23.15 renin

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Results	in table
1	Activating Compound
205	AA Sequence
26	Application
1	CAS Registry Number
23	Cloned(Commentary)
9	Crystallization (Commentary)
38807	Disease/ Diagnostics
17	Expression
6	General Information
8	General Stability
283	IC50 Value
452	Inhibitors
3	kcat/KM [mM/s]
38	Ki Value [mM]
21	KM Value [mM]
15	Localization
41	Molecular Weight [Da]
65	Natural Substrates/ Products (Substrates)
171	Organism
191	PDB ID
17	pH Optimum
3	pH Range
1	pH Stability
23	Posttranslational Modification
6	Protein Variants
30	Purification (Commentary)
2	Reaction
1	Reaction Type
171	Reference
123	Source Tissue
40	Specific Activity [micromol/min/mg]
12	Storage Stability
111	Substrates and Products (Substrate)
12	Subunits
15	Synonyms
3	Temperature Optimum [°C]
8	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.23.15 - renin

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Homo sapiens

95753, 95783, 95804, 95809

hanging drop vapor diffusion method, recombinant renin. Crystal structure of recombinant renin in complex with 5-[4-[(3,5-difluorobenzyl)amino]phenyl]-6-ethylpyrimidine-2,4-diamine, 6-ethyl-5-[1-(3-methoxypropyl)-2-phenyl-1,2,3,4-tetrahydroquinolin-7-yl]pyrimidine-2,4-diamine, and N-[2-([2-amino-6-ethyl-5-[4-(3-methoxypropyl)-2,2-dimethyl-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-6-yl]pyrimidin-4-yl]amino)ethyl]naphthalene-2-sulfonamide

Homo sapiens

677527

in complex with angiotensinogen, sitting drop vapor diffusion method, using 1.74 M (NH4)2SO4 and 0.1 M Tris, pH 7.6

Homo sapiens

P00797

754182

in complex with the (+)- and (-)-enantiomer of inhibitor 7-[4-[3-(2-chloro-3,6-difluorophenoxy)propyl]phenyl]-N-cyclopropyl-N-(2,3-dichlorobenzyl)-3,9-diazabicyclo[3.3.1]non-6-ene-6-carboxamide. The hydrophobic interactions dominate the positioning of the inhibitors with the pseudosymmetry of the central template being able to establish the necessary hydrogen bonds in either orientation. Substitution of either of the two nitrogen atoms abolishes this pseudosymmetry and completely abrogates this observed effect

Homo sapiens

P00797

699465

modeling of stereo structure of the complex of human renin with dipeptide YY. The loss of inhibitory activiy at basic pH values may be due to a local shift of YY from the center of the renin cleft into the N-domain side