Jasper Small Lactate Sandbox 1

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==Reference==
==Reference==
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<ref group="xtra">PMID:11276087</ref><references group="xtra"/>
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1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm
1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm
2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf
2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf

Revision as of 09:20, 3 March 2010

PDB ID 1i10

Drag the structure with the mouse to rotate
1i10, resolution 2.30Å ()
Ligands: , ,
Gene: LDHA (Homo sapiens)
Activity: L-lactate dehydrogenase, with EC number 1.1.1.27
Related: 1i0z, 9ldt, 5ldh, 1ldg
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Contents

HUMAN MUSCLE L-LACTATE DEHYDROGENASE M CHAIN, TERNARY COMPLEX WITH NADH AND OXAMATE

Lactate Dehydrogenase

Lactate Dehydrogenase (LDH) is an important enzyme in humans. It occurs in different regions of the body, each region having a unique conformation of different subunits. The Jmole image shown is that of LDH-5, the form found in skeleton muscle and the liver.

Function

Catalytic function of LDH (1)
Catalytic function of LDH (1)

LDH preforms an important metabolic function in the body. The enzyme catalyzes both the conversion of pyruvate to lactose as well as the conversion of lactose to pyruvate. The conversion of pyruvate to lactose occurs in the muscles of the body when oxygen is absent. The lactate acid is then moved back to the liver where LDH catalyzes the Cori cycle which converts the lactose back into pyruvate. The reaction is also important as it is coupled with the interconversion of NADH and NAD+.


Catalysis

Studies have shown that the reaction mechanism of LDH follows an ordered sequence. In order for lactate to be oxidized NAD+ must bind to the enzyme first followed by lactate. Transfer of a hydride ion then happens quickly in either direction giving a mixture of the two teranary complexes, enzyme-NAD+-lactate and enzyme-NADH-pyruvate. Finally pyruvate dissociates from the enzyme followed by NADH. The rate limiting step in this reaction is the rate of dissociation of NADH. The same holds true in the reverse reaction that the coenzyme, NADH, must bind first before the substrate, pyruvate, can bind. The conversion of pyruvate to lactate with the subsequent regeneration of NAD+ is a very favorable(1).

(1)
(1)

Important Sites:

Structure

LDH is comprized of 40% alpha helixes and 23% beta sheets.(2)

SCOP 1I10- a/b Mainly parallel beta sheets (beta-alpha-beta units) 1I0Z- a/b Mainly parallel beta sheets (beta-alpha-beta units)

Reference

1- http://www.bioc.aecom.yu.edu/labs/calllab/highlights/LDH.htm 2- http://www.cheric.org/ippage/e/ipdata/2004/05/file/e200405-701.pdf

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